ДЕТЕРГЕНТНАЯ КОМПОЗИЦИЯ

Настоящее изобретение относится к биохимии и представляет собой детергентную композицию, которая включает вариант субтилизина, имеющий аминокислотную последовательность, которая приведена в SEQ ID NO 1, и по меньшей мере один дополнительный ингредиент, выбранный из: i) средств для отбеливания, которые выбраны из перкарбонатов, персульфатов и органических надкислот, ii) аминокарбоксилатов, или iii) сульфированных полимеров, или iv) фосфорорганических кислот или их солей и их смесей. Изобретение также относится к способу удаления или уменьшения загрязнений белковоподобных веществ с поверхностей, имеющих подобные загрязнения, с использованием указанной композиции. Указанная композиция дает хорошие результаты при удалении загрязнений белковоподобных веществ, даже в составах с щелочными значениями рН. 2 н. и 18 з.п. ф-лы, 2 табл., 2 пр.

ДЕТЕРГЕНТНАЯ КОМПОЗИЦИЯ

Изобретение относится к дисперсной детергентной композиции, где композиция содержит поверхностно-активное вещество и/или моющий компонент, протеазу и ингибитор протеазы. При этом протеаза представляет собой субтилизин или 10R протеазу, где протеаза присутствует в концентрации 1Е-09 - 2Е-03 моль/кг детергента, отношение ингибитора к протеазе составляет 0,1-1000 моль ингибитора/моль протеазы, и где ингибитор протеазы представляет собой пептидный альдегид. Варианты пептидных альдегидов приведены в формуле изобретения. Техническим результатом заявленного изобретения является получение детергентной композиции с увеличенной моющей способностью протеазы. Изобретение также относится к способу получения указанной детергентной композиции, к применению композиции для стирки загрязненных изделий и к способу удаления яичного загрязнения. 5 н. и 14 з.п. ф-лы, 4 пр.

ВАРИАНТ СУБТИЛИЗИНА BACILLUS (ВАРИАНТЫ), КОДИРУЮЩАЯ ЕГО ДНК, ЭКСПРЕССИРУЮЩИЙ ВЕКТОР И ОЧИЩАЮЩАЯ КОМПОЗИЦИЯ

Изобретение относится к области генной и белковой инженерии и может быть использовано при создании новых моющих средств и очищающих составов. Предложены мутантные формы субтилизина Bacillus, являющиеся результатом определенной комбинации замен в аминокислотной последовательности нативного фермента, от которой они происходят, и отличающиеся от субтилизина-предшественника повышенной эффективностью очищающего действия. Все варианты субтилизина по изобретению характеризуются либо заменой валином остатка в положении, соответствующем положению 232 аминокислотной последовательности субтилизина Bacillus amyloliquifaciens, либо заменой пролином остатка в положении 212 указанной природной формы субтилизина. Для получения предложенных новых форм фермента соответствующие мутантные последовательности ДНК экспрессированы в клетках-хозяевах, предпочтительно в клетках штаммов Bacillus с пониженным уровнем активности протеаз. Приобретаемые вариантами субтилизина в результате модификации свойства обеспечивают ...

КОМПОЗИЦИЯ СРЕДСТВА ДЛЯ СТИРКИ, СОДЕРЖАЩАЯ ГЛИКОЗИЛГИДРОЛАЗУ

Настоящее изобретение относится к композиции средства для стирки, содержащей гликозилгидролазу, обладающую ферментативной активностью по отношению как к ксилоглюкановым, так и к аморфным целлюлозным субстратам, где гликозилгидролазу выбирают из семейств GH 5, 12, 44 или 74; (ii) 0,05-10% мас. амфифильного алкоксилированного жироудаляющего полимера и (iii) 2-50% мас. моющего поверхностно-активного вещества. Также настоящее изобретение относится к композиции средства для стирки, содержащей: (i) гликозилгидролазу, обладающую ферментативной активностью по отношению как к ксилоглюкановым, так и к аморфным целлюлозным субстратам, где гликозилгидролазу выбирают из семейств GH 5, 12, 44 или 74; (ii) статистический привитой сополимер, содержащий: (a) гидрофильную основную цепь, содержащую мономеры, выбранные из группы, состоящей из: спиртов, алкоксильных звеньев и малеинового ангидрида; и (b) гидрофобную боковую цепь (цепи), выбранную из группы, состоящей из: сложного винилового эфира насыщенной ...

МОЮЩИЕ СРЕДСТВА СО СТАБИЛИЗИРОВАННЫМИ ФЕРМЕНТНЫМИ СИСТЕМАМИ

Изобретение относится к очищающей, отбеливающей или дезинфицирующей композиции, представляющей собой стабилизированную оксидазную композицию, содержащую указанную оксидазу и стабилизатор и по меньшей мере один субстрат указанной оксидазы, где указанный стабилизатор содержит по меньшей мере один ингибитор оксидазы, причем указанный стабилизатор выбирают из тиосульфата и 2-амино-2-метил-1-пропанола. В некоторых особенно предпочтительных вариантах осуществления изобретения указанную оксидазу выбирают из глюкозооксидазы, сорбитоксидазы, холиноксидазы, гексозооксидазы и спиртовой оксидазы. Изобретение также относится к способу образования отбеливающего продукта в моющем растворе, включающему стадию добавления указанной композиции к указанному моющему раствору, где в предпочтительном варианте осуществления указанный отбеливающий продукт представляет собой пероксид или отбеливающую систему, которую можно активировать с помощью пероксида. Техническим результатом изобретения является обеспечение ...

МНОГОФАЗНАЯ ТАБЛЕТКА МОЮЩЕГО СРЕДСТВА И СПОСОБ МЫТЬЯ В ПОСУДОМОЕЧНОЙ МАШИНЕ

Изобретение относится к многофазным таблеткам моющего средства для посудомоечной машины, а также к способу их применения. Указанная таблетка содержит а) первую фазу в виде сформированного тела, имеющего в себе, по меньшей мере, одну пресс-форму, и б) вторую фазу в виде спрессованной формы, содержащейся за счет адгезии в указанной пресс-форме, где композиция таблетки включает один или более агентов с активностью моющего средства, которые сконцентрированы преимущественно во второй фазе, и где вторая фаза дополнительно включает связующее, при этом сформированное тело первой фазы получают при давлении прессования, по меньшей мере, приблизительно 350 кг/см2, а вторую фазу прессуют при давлении, меньшем чем приблизительно 350 кг/см2. Технический результат - прекрасные растворение и характеристики мытья наряду с надлежащей целостностью и прочностью таблеток. 2 с. и 4 з.п.ф-лы, 1 табл.

МНОГОФАЗНАЯ ДЕТЕРГЕНТНАЯ ТАБЛЕТКА, СПОСОБ МЫТЬЯ В МОЕЧНОЙ МАШИНЕ

Изобретение относится к многофазным детергентным таблеткам, а также к способу их применения в моечных машинах. Указанная таблетка содержит: а) первую фазу в виде сформированного тела, содержащего, по крайней мере, одну форму, и б) вторую фазу в виде спрессованного тела, содержащегося внутри указанной формы за счет адгезии, причем композиция таблетки содержит одно или более детергентных активных веществ, сконцентрированных преимущественно во второй фазе и где вторая фаза дополнительно содержит разрушающий агент, при этом сформированное тело первой фазы получают при давлении прессования, по крайней мере, около 350 кг/см2, а вторую фазу прессуют при давлении менее чем около 350 кг/см2. Технический результат - прекрасные характеристики растворимости и чистящих свойств, наряду с хорошей целостностью и прочностью таблеток. 2 н. и 10 з.п.ф-лы.

САЛФЕТКА С УСИЛЕННЫМ МОЮЩИМ СРЕДСТВОМ ДЛЯ СТИРКИ С ТЕМПЕРАТУРНО-ЗАВИСИМОЙ АКТИВАЦИЕЙ МОЮЩИХ АКТИВНЫХ ВЕЩЕСТВ

Изобретение относится к салфеткам с усиленным моющим средством для стирки. Описан способ получения салфетки с усиленным моющим средством для стирки, характеризующийся следующими стадиями: (a) введение доноров кислорода и их активаторов в восковую матрицу, окруженную слоем ионного полимера, для обеспечения капсульной системы, (b) введение капсульной системы в дисперсию, содержащую жидкое моющее средство, ферменты и нерастворимую в воде функциональную добавку, содержащую цеолит и/или филлосиликат, и (c) нанесение дисперсии с капсульной системой на несущий материал, являющийся твердым при комнатной температуре. Технический результат – обеспечение усиленного моющего эффекта при стирке. 3.н. и 3 з.п. ф-лы, 2 ил.

СИНТЕТИЧЕСКОЕ МОЮЩЕЕ СРЕДСТВО "АОС"

Изобретение относится к составам порошкообразных синтетических моющих средств (CMC) и предназначено как для ручной, так и для машинной стирки и замачивания всех видов текстильных изделий, в том числе и цветных, и других бытовых нужд. Сущность: средство содержит следующие компоненты в мас.%: анионное ПАВ - алкилбензолсульфонат натрия 10-16; неионогенное ПАВ - оксиэтилированные жирные спирты или оксиэтилированный алкилфенол 2-5; триполифосфат натрия 15-25; органофосфонатное соединение - натриевая соль 1-гидроксиэтилиден фосфоновой кислоты или диэтилентриаминопентаксис-(метиленфосфонат) натрия 0,2-0,6; поликарбоксилат 0,5-1,5; карбоксиметилцеллюлоза 0,3-0,6; модифицированный полиалкиленгликоль 0,2-0,6; оптический отбеливатель 0,05-0,3; кальцинированная сода 3-6; жидкое стекло 3,5-6,0; энзим 0,4-0,7; пеногаситель 0,05-1,5; отдушка 0,15-0,3; сульфат натрия и вода до 100. Технический результат - повышение эффективности моющего средства с отбеливающим эффектом, удаление всех видов загрязнений ...

СТАБИЛЬНОЕ ПРИ ХРАНЕНИИ ЖИДКОЕ МОЮЩЕЕ ИЛИ ЧИСТЯЩЕЕ СРЕДСТВО, СОДЕРЖАЩЕЕ ПРОТЕАЗУ И ЦЕЛЛЮЛАЗУ

Изобретение относится к области биохимии. Представлено применение модифицированной протеазы в качестве средства для повышения стабильности при хранении целлюлазы в жидком моющем или чистящем средстве, включающем целлюлазу и протеазу. Изобретение обеспечивает пониженную дезактивацию целлюлазы посредством вышеуказанной протеазы, тем самым позволяя сохранить высокую целлюлолитическую остаточную активность в указанном моющем или чистящем средстве даже после 8 недель хранения. 7 з.п. ф-лы, 2 табл., 1 пр.

Композиции, содержащие липазы, и способы обработки поверхности

Изобретение относится к композициям, содержащим липазные ферменты и отбеливающие агенты, а также к способам получения и использованию таких композиций. Описан способ очистки ткани, или твердой поверхности, или другой поверхности при уходе за тканями и бытовом уходе, включающий стадии, на которых: (a) вводят в контакт поверхность с водным раствором, содержащим (i) липазу; и (ii) отбеливающий компонент и (iii) необязательное моющее вспомогательное вещество; (b) промывают и высушивают ткань или твердую поверхность; при этом липаза включает вариант родительской липазы, причем родительская липаза содержит аминокислотную последовательность с, по меньшей мере, 60% идентичностью со зрелым полипептидом SEQ ID NO: 1 и причем вариант липазы имеет аминокислотную последовательность с, по меньшей мере, 60% идентичностью со зрелым полипептидом SEQ ID NO: 1, или его фрагмент, имеющий липазную активность, причем указанный вариант содержит следующие замены: (a) G91A+D96G+T231R+N233R; (b) T37R+N39R+G91A+D96G ...

ВАРИАНТЫ АЛЬФА-АМИЛАЗЫ С ИЗМЕНЕННЫМИ СВОЙСТВАМИ

Настоящее изобретение относится к области биотехнологии и может быть использовано в производстве композиций, предназначенных для удаления крахмалсодержащих загрязнений. Предложены композиции, содержащие активные варианты альфа-амилазы, которые проявляют повышенную термостабильность относительно родительской формы AmyS-подобной альфа-амилазы, из которой они получены путем замены S/Q в положении, соответствующем положению 242 альфа-амилазы с SEQ ID NO: 1. Помимо нового варианта альфа-амилазы композиции по изобретению обычно содержат, по меньшей мере, один дополнительный фермент, детергент, одно поверхностно-активное вещество, один комплексообразователь, окислитель, подкислитель, подщелачивающий агент, источник пероксида, источник жесткости, соль, детергентный комплексообразующий агент, полимер, стабилизирующий агент или кондиционер. Описаны также способы применения этих композиций для расшлихтовки тканого материала, для мойки или очистки изделий, таких как посуда или белье, загрязненных крахмалсодержащими ...

КОМПОЗИЦИИ, СОДЕРЖАЩИЕ ФЕРМЕНТ И ОТТЕНОЧНЫЙ АГЕНТ ДЛЯ ТКАНИ

Изобретение относится к композициям, содержащим определенные варианты липаз и оттеночный агент для ткани, и включает использование таких композиций для очистки и/или обработки участков поверхностей или тканей, с обеспечением улучшенного отложения оттеночного красителя, снижения активности фермента, приводящей к появлению неприятного запаха, и ощущения чистоты. 16 з.п. ф-лы, 3 табл.

ЭЛЕКТРОЛИТИЧЕСКАЯ СИСТЕМА ДЛЯ АВТОМАТИЧЕСКОГО МЫТЬЯ ПОСУДЫ

Изобретение относится к способу автоматического мытья посуды. Описан способ автоматического мытья посуды, включающий электролитическое получение отбеливающих соединений, мытье посуды композицией, включающей отбеливающие соединения, и последующее мытье посуды композицией, включающей фермент, причем электролитическое получение отбеливающих соединений проводят при температуре не выше 40°C. Технический результат - обеспечение высокой отбеливающей способности и производительности. 5 з.п. ф-лы, 1 табл.

КОНЦЕНТРАТ ОЧИСТИТЕЛЯ ДЛЯ ОЧИСТКИ МЕДИЦИНСКИХ И/ИЛИ ХИРУРГИЧЕСКИХ ИНСТРУМЕНТОВ И/ИЛИ АППАРАТУРЫ И СПОСОБ ЕГО ПРИМЕНЕНИЯ

Изобретение относится к концентрату очистителя для очистки медицинских и/или хирургических инструментов и/или аппаратуры, содержащему по крайней мере одно ионное поверхностно-активное вещество, по крайней мере один солюбилизатор, по крайней мере один обычный протеолитический энзим и воду, отличающийся тем, что в качестве ионного поверхностно-активного вещества он содержит соль (С5-С12) алкилсульфата и дополнительно содержит по крайней мере один алканоламин при следующем соотношении компонентов, вес.%: соль (С5-С12 ) алкилсульфата 0,5-8,0, солюбилизатор 4,0-15,0, алканоламин 4,0-10,0, протеолитический энзим в количестве 0,005-0,1 Энсон ед/г очистителя, вода - до 100. Описывается также способ очистки медицинских и/или хирургических инструментов. Технический результат - повышение эффективности очистки. 2 с. и 9 з.п. ф-лы, 4 ил.

МОДИФИЦИРОВАННЫЙ СУБТИЛИЗИН, ДНК, КОДИРУЮЩАЯ МОДИФИЦИРОВАННЫЙ СУБТИЛИЗИН, ВЕКТОР ЭКСПРЕССИИ, КОДИРУЮЩИЙ ДНК, И ШТАММ КУЛЬТУРЫ КЛЕТКИ ХОЗЯИНА

Изобретение характеризует модифицированную карбонилгидролазу. В аминокислотной последовательности субтилизина заменены 76 аминокислотный остаток и по меньшей мере еще один аминокислотный остаток. Модификация позволяет повысить протолитическую активность фермента. 4 с. и 7 з.п. ф-лы, 10 ил., 7 табл.

СПОСОБ УДАЛЕНИЯ ИЗБЫТОЧНОГО КРАСИТЕЛЯ С НАБИВНОЙ ИЛИ ОКРАШЕННОЙ ТКАНИ ИЛИ ПРЯЖИ

Изобретение относится к области красильно-отделочного производства, в частности, к способу удаления избыточного красителя с набивной или окрашенной ткани или пряжи, включающему обработку раствором для полоскания, содержащим, по меньшей мере, один фермент, проявляющий пероксидазную или лакказную активность, в концентрации от 0,005 до 5 мг белка фермента на 1 л раствора для полоскания, окислитель, медиатор - 1-гидроксибензтриазол в концентрации от 1 мкМ до 1 мМ и, необязательно, добавки. Предлагаются также система для удаления избыточного красителя с набивной или окрашенной ткани или пряжи и композиция для ее приготовления. Изобретение способствует удалению избыточного красителя с набивной или окрашенной ткани или пряжи без отбеливания окрашенной или набивной ткани. 3 с. и 24 з.п.ф-лы.

ПОРОШКОВОЕ МОЮЩЕЕ СРЕДСТВО

Порошковое моющее средство содержит, мас.%: смесь анионного и неионогенного поверхностно-активных веществ 10 - 20; комплексообразователь дифонат 5 - 10; цеолит 0,01 - 10 и/или натрий триполифосфат 0,01 - 20; натрий двууглекислый 5 - 15; стекло натриевое жидкое 1 - 10,0; натрий карбоксиметилцеллюлоза 0,5 - 2; оптические отбеливатели 0,05 - 0,15; щелочная протеаза 0,5 - 2; комплексный CO2 -экстракт или гидрофитоконцентрат из смеси хмеля и ростков ячменя или комплексный CO2 -экстракт или гидрофитоконцентрат из смеси семян моркови и ростков ячменя 0, 001 - 1; CO2 -экстакт или гидрофитоконцентрат конопли или CO2 -экстракт или гидрофитоконцентрат виноградных семян 0,001 - 1; CO2 -экстракт мяты или ментол или смесь CO2 -экстракта мяты и ментола в массовом соотношении 2 : 1 - 0,001 - 0,5; отдушка 0,05 - 0,5; сульфат натрия и вода до 100. 2 табл.

Гранулированное моющее средство и способ его производства

Группа изобретений относится к гранулированному моющему средству. Способ производства гранулированного моющего средства включает подготовку основы, для чего в емкости нагревают высокомолекулярный полиэтиленгликоль и жирную кислоту С12 до температуры 80-90°C, затем при постоянном перемешивании добавляют натриевую соль угольной кислоты, полученную основу перемешивают до полного растворения натриевой соли угольной кислоты и добавляют C12-18 Alcohol ethoxylate, далее основу перемешивают до однородной массы и добавляют натриевую соль метилового эфира альфа-олефин сульфоната и перемешивают до полного растворения, затем добавляют минеральный наполнитель при этом температуру основы поддерживают на уровне 55-60°C, в отдельной емкости перемешивают низкомолекулярный полиэтиленгликоль, краситель, энзимы, эфирное масло, отдушку, ароматическую композицию с пролонгированным высвобождением аромата и оптический отбеливатель и добавляют к подготовленной основе, все перемешивают при температуре 55-60°C, затем ...

СПОСОБ ИЗМЕНЕНИЯ, ДЕСТРУКЦИИ ИЛИ ОТБЕЛИВАНИЯ ЛИГНИНА, ЛИГНИНСОДЕРЖАЩЕГО МАТЕРИАЛА ИЛИ ПОДОБНЫХ ВЕЩЕСТВ

Способ предназначен для изменения, деструкции или отбеливания лигнина, лигнинсодержащего материала или подобных веществ при обработке в реакционном растворе при использовании катализаторов окисления и пригодных окислителей. Эти катализаторы используют в комбинации с алифатическими, циклоалифатическими, гетероциклическими или ароматическими, содержащими NO-, NOH- или соединениями. Заявленный способ обладает значительно лучшей производительностью, чем известные способы. 32 з.п.ф-лы, 2 табл.

Уплотненная композиция жидкого моющего средства для стирки

Настоящее изобретение относится к композиции жидкого моющего средства для стирки. Описана композиция жидкого моющего средства для стирки, содержащая: (a) жидкую фазу; (b) твердые частицы фермента, составляющие от 0,5 до 15% по массе композиции жидкого моющего средства, при этом твердая фаза диспергирована в жидкой фазе и при этом водорастворимую твердую фазу определяют как твердое вещество, полученное при центрифугировании композиции жидкого моющего средства для стирки при 1200 g в течение 10 мин; и при этом жидкая фаза содержит спирт, составляющий от 5 до 40% по массе композиции, который выбирают из группы, содержащей этиленгликоль, 1,3-пропандиол, 1,2-пропандиол, тетраметиленгликоль, пентаметиленгликоль, гексаметиленгликоль, 2,3-бутандиол, 1,3-бутандиол, диэтиленгликоль, триэтиленгликоль, полиэтиленгликоль, глицеринформаль, дипропиленгликоль, полипропиленгликоль, н-бутиловый простой эфир дипропиленгликоля и их смеси, предпочтительно спирт выбирают из группы, содержащей 1,2-пропандиол, ...

НОВЫЙ АМИЛОЛИТИЧЕСКИЙ ФЕРМЕНТ ИЗ BACILLUS SP.А7-7(DSM12368), А ТАКЖЕ МОЮЩЕЕ И ЧИСТЯЩЕЕ СРЕДСТВО С ЭТИМ НОВЫМ АМИЛОЛИТИЧЕСКИМ ФЕРМЕНТОМ

... 1. Амилолитический белок с аминокислотной последовательностью, идентичной приведенной в SEQ ID NO. 2 аминокислотной последовательности не менее чем на 96%. 2. Амилолитический белок с аминокислотной последовательностью, идентичной приведенной в SEQ ID NO. 2 аминокислотной последовательности не менее чем на 98%. 3. Амилолитический белок с аминокислотной последовательностью, идентичной приведенной в SEQ ID NO. 2 аминокислотной последовательности по позициям от 32 до 516 не менее чем на 96%. 4. Амилолитический белок с аминокислотной последовательностью, идентичной приведенной в SEQ ID NO. 2 аминокислотной последовательности по позициям от 32 до 516 не менее чем на 98%. 5. Амилолитический белок, кодируемый нуклеотидной последовательностью, идентичной приведенной в SEQ ID NO. 1 нуклеотидной последовательности не менее чем на 85%, в частности по его участку, соответствующему аминокислотам от 32 до 516 в соответствии с SEQ ID NO. 2. 6. Амилолитический белок, кодируемый нуклеотидной последовательностью ...

ОЧИЩАЮЩЕЕ СРЕДСТВО

... 1. Жидкий состав моющего или очищающего средства A, включающий a) >5 мас.% по меньшей мере одного обладающего моющим или очищающим действием фермента; b) >5 мас.% по меньшей мере одного органического растворителя; c) борная кислота или производное борной кислоты d) источник ионов Ca или Mg.2. Жидкий состав моющего или очищающего средства по п.1, отличающийся тем, что он содержит обладающий моющим или очищающим действием фермент из группы амилаз и/или протеаз.3. Жидкий состав моющего или очищающего средства по п.2, отличающийся тем, что он в каждом случае по отношению к полной массе состава моющего или очищающего средства содержит от 0,1 до 30 мас.%, предпочтительно от 1,0 до 25 мас.% и, в частности, от 2,0 до 20 мас.% состава амилазы.4. Жидкий состав моющего или очищающего средства по п.2, отличающийся тем, что он в каждом случае по отношению к полной массе состава моющего или очищающего средства содержит предпочтительно от 5 до 50 мас.%, предпочтительно от 7 до 40 мас.% и, в частности, ...

ДЕТЕРГЕНТНАЯ КОМПОЗИЦИЯ

... 1. Дисперсная детергентная композиция, которая содержит поверхностно-активное вещество и/или моющий компонент, протеазу и ингибитор протеазы.2. Детергентная композиция по п.1, которая содержит ингибитор в количестве, эффективном для увеличения моющей способности или стабильности протеазы при стирке в растворе детергента.3. Детергентная композиция по п.1, которая представляет собой детергент для мытья посуды, содержащий моющий компонент.4. Детергентная композиция по п.3, которая содержит больше 5% моющего компонента.5. Детергентная композиция по п.1, где моющий компонент представляет собой хелатирующее средство, которое образует водорастворимые комплексы с Ca и Mg, и где комплекс с Ca и/или Mg имеет константу устойчивости в диапазоне log K=3-8.6. Детергентная композиция по п.1, где моющий компонент содержит аминогруппу, в частности, одну, две или три аминогруппы.7. Детергентная композиция по п.3 или 4, где моющий компонент представляет собой MGDA, GLDA, NTA или DTPA.8. Детергентная композиция ...

Детергентная композиция для предотвращения удаления красителя и перенос красителя, обладающая повышенной способностью к удалению пятен, въевшихся в ткань

ЖИДКОЕ МОЮЩЕЕ СРЕДСТВО

ГРАНУЛИРОВАННАЯ МОЮЩАЯ КОМПОЗИЦИЯ С ЛИПАЗОЙ, СПОСОБ ОЧИСТКИ ТКАНЕЙ

Изобретение относится к гранулированной моющей композиции, содержащей: (а) от 0,00025 до 0,015 г активного фермента определенных липаз на 100 г композиции, (b) от 0,5 до 10 мас.% алкилалкоксисульфата или амида полиокси жирной кислоты, (с) от 2 до 30 мас.% дополнительного анионного или неионогенного поверхностно-активного вещества, где соотношение а / b равно 0,09 - 0,28, с улучшенными свойствами после первого цикла стирки. Представлен также способ стирки тканей.

ОЧИЩАЮЩИЕ ФЕРМЕНТЫ И УСТРАНЕНИЕ НЕПРИЯТНОГО ЗАПАХА

... 1. Очищающая композиция, содержащая: ! а) ацилтрансферазу и ! b) спиртовой субстрат для указанной ацилтрансферазы; ! где указанная ацилтрансфераза и спиртовой субстрат присутствуют в количестве, эффективном для продукции детектируемого сложного эфира после объединения указанной очищающей композиции с донором ацила. ! 2. Композиция по п.1, где указанной ацилтрансферазой является SGNH-ацилтрансфераза. ! 3. Очищающая композиция по п.1, которая дополнительно содержит: ! с) донор ацила и ! d) сложный эфир, продуцирующийся в результате реакции взаимодействия указанного спиртового субстрата и указанного донора ацила, катализируемой указанной ацилтрансферазой. ! 4. Композиция по п.3, где указанной ацилтрансферазой является SGNH-ацилтрансфераза. ! 5. Очищающая композиция по п.3, где указанным сложным эфиром является средство для ухода за тканью. ! 6. Очищающая композиция по п.5, где указанным средством для ухода за тканью является сложноэфирное поверхностно-активное вещество. ! 7. Способ по п.3, ...

КОМПОЗИЦИЯ НА ОСНОВЕ ЛИПАЗЫ И БЕТА-ЦИКЛОДЕКСТРИНОВ ДЛЯ РЕГУЛЯЦИИ КИНЕТИКИ ЭНЗИМАТИЧЕСКОГО РАСЩЕПЛЕНИЯ ЖИРА И МЫТЬЯ ПОВЕРХНОСТЕЙ

Группа изобретений относится к бытовой химии. Композиция, предназначенная для использования в средстве бытовой химии, содержит липазу и β-циклодекстрин, где массовое соотношение липазы и β-циклодекстрина составляет (0,0025-0,25):(0,1-1) соответственно, причем указанная липаза находится в водно-глицериновом растворе, представляющем собой коммерчески доступный продукт Lipex® Evity® 200 L, модифицированный дополнительным количеством глицерина. Также раскрыты другой вариант композиции для использования в средстве бытовой химии, средство бытовой химии и применение композиции для регуляции кинетики энзиматического расщепления липидов и нейтрализации неприятных запахов, поддержания длительной чистоты и приятного аромата. Группа изобретений обеспечивает эффективную регуляцию кинетики энзиматического расщепления липидов с одновременной эффективной нейтрализацией неприятных запахов на различных типах поверхностей. 4 н. и 20 з.п. ф-лы, 5 табл., 6 пр.

Способ получения гранулированного ферментсодержащего моющего средства

DETERGENT FOR WASHING

TEXTILWASCHMITTEL ENTHALTEND LIPOLYTISCHES ENZYM UND AMINVERBINDUNGEN

Waschmittelzusammensetzungen zur Verhinderung der Farbstoffübertragung

SCHMUTZABWEISUNGSMITTEL ENTHALTENDE WASCHMITTELZUSAMMENSETZUNGEN

ENZYMDISPERSIONEN, DEREN HERSTELLUNG UND DIESE ENTHALTENDE ZUSAMMENSETZUNGEN

Neuartige Lipasevarianten zur Verwendung in Reinigungsmitteln

NAPHTHALINBORONSÄUREN

Reinigungsgemisch zur Entfernung beziehungsweise Vermeidung von Insektenablagerungen auf Oberflächen

Die Erfindung betrifft ein Reinigungsgemisch zur Entfernung beziehungsweise Vermeidung von Insektenablagerungen auf Oberflächen, umfassend mindestens eine Protease in Kombination mit mindestens einer Chitinase und mindestens ein kompatibles Tensid.

Waschmittelzusammensetzungen mit Zusätzen zur Verhinderung der Farbstoffübertragung

THERMOSTABILE PROTEASE AUS THERMOBACTEROIDES

Antimikrobielles Verfahren und Formulierung unter Verwendung von Endoglycosidase vom Typ II und antimikrobielles Mittel

Verfahren und Formulierung unter Verwendung von Endoglycosidase vom Typ II

WASSERLOESLICHE MIKROKAPSELN.

Die Farbstoffübertragung hemmende Waschmittelzusammensetzungen

ALKALISCHE PROTEASE UND VERFAHREN ZU IHRER HERSTELLUNG

VERBESSERTE SACCHARIFIZIERUNG VON ZELLULOSE DURCH KLONIERUNG UND VERVIELFÄLTIGUNG DES BETA-GLUKOSIDASE GENES AUS TRICHODERMA REESEI

Polymerzusammensetzungen

Pseudomonas isomerase enzyme

A Pseudomonas enzyme that catalyses cis/trans isomerisation of unsaturated fatty acids is new, especially an enzyme derived from P. putida DDSM 11306. Also claimed is the gene coding for the enzyme, and a host organism containing the gene.

Phosphatfreies flüssiges Geschirrspülmittel

Die vorliegende Erfindung betrifft ein phosphatfreies, flüssiges Geschirrspülmittel das eine verbesserte Stabilität und Reinigungsleistung insbesondere an enzymsensitiven Anschmutzungen zeigt, die Verwendung dieses Geschirrspülmittels sowie ein Verfahren zum maschinellen Geschirrspülen unter Verwendung dieses Geschirrspülmittels.

Flüssige Tensidzusammensetzung mit spezieller Kombination aus Enzym und Stabilisator

Thermostabile Wasch- oder Reinigungsmittel sind dadurch gekennzeichnet, dass sie a) mindestens eine Protease enthält, die eine Aminosäuresequenz umfasst, die zu der in SEQ ID NO. 1 angegebenen Aminosäuresequenz über deren Gesamtlänge zu mindestens 90% und zunehmend bevorzugt zu mindestens 90,5%, 91%, 91,5%, 92%, 92,5%, 93%, 93,5%, 94%, 94,5%, 95%, 95,5%, 96%, 96,5%, 97%, 97,5%, 98%, 98,5% und 99% identisch ist, und Substitutionen an mindestens einer der Positionen 3, 4, und/oder 199, vorzugsweise die Aminosäuresubstitutionen S3T, V4I und V199I bezogen auf SEQ ID NO:1 aufweist, und b) Borat in einer Menge von 0,5–5 Gew.-%, bevorzugt 1%–4 Gew.-%, besonders bevorzugt 1,5–3 Gew.-% enthalten.

Reinigungsmittel-Tablette

VERFAHREN ZUR ERZEUGUNG EINES STRUKTUREFFEKTES AUF TEXTILEN FLÄCHENGEBILDEN

PROZESS ZUM BEHANDELN VON TEXTILEN FASERMATERIALIEN

Bleichmittel

Frei fliessendes Pulverpraeparat zur enzymatischen Behandlung tierischer oder pflanzlicher Werkstoffe

MUTANTEN DER alpha-AMYLASE

Lipasehaltiges Textilwaschmittel

The invention concerns a lipase-containing detergent which, whilst having the minimum possible lipase content, has a performance which at least matches that of an agent containing conventional lipases. In addition to conventional components, the detergent comprises a lipolytically active amount of a lipase which is optionally altered by genetic engineering and which is derived from Pseudomonas alcaligenes or Pseudomonas pseudoalcaligenes. The lipase further has a molecular weight of 30 kD to 32 kD, an isoelectric point ranging from 4.5 to 6, and a specific activity of 900 DLU/mg to 1000 DLU/mg.

Parfümierte Waschmittelzusammensetzungen

CELLULASEZUSAMMENSETZUNGEN MIT EINEM DEFIZIT AN KOMPONENTEN DES TYPS-CBH I ENTHALTENDE REINIGUNGSMITTELZUSAMMENSETZUNGEN

ENZYME UND WASCHMITTELZUSAMMENSETZUNGEN AUF ENZYMBASIS

MUTIERTE ALKALISCHE CELLULASE

Verfahren und Zusammensetzung zur Reinigung und Desinfektion von Kontaktlinsen.

Kombiniertes zweistufiges Verfahren zum Reinigen und Entseuchen von chirurgischen Instrumenten

MEHRFACH SUBSTITUIERTE PROTEASEVARIANTEN

Granular enzymic washing powder prodn

A mixture of enzyme (1-30 pbw), NaHPO4, (33-53), water (47-65), Na polyphosphate (50-150) is spray-dried at 35-80 degrees C (pref. 40-70 degrees C) into a chamber below 40 degrees C. The Na polyphosphate (50-150) is composed of Na4P2O7 (4-100) and Na5P3O10. The solids content of the mixture to be sprayed is pref. about 75%. Optional additions include non-ionic surfactant 0.1-15 and hydrotropic substances (e.G., Na benzene sulphonate) 0.1-15 parts by weight. Solid additives may be added after drying.

VERFAHREN ZUR HERSTELLUNG VON PULVERFOERMIGEN ENZYMPRAEPARATEN UND VORRICHTUNG ZUR DURCHFUEHRUNG DES VERFAHRENS

Dishwashing detergent in the form of a molded body, useful for improved removal of starch containing stains, comprises polyvinylpyrrolidone particles and an amylase preparation

Dishwashing detergent in the form of a molded body, comprises polyvinylpyrrolidone particles and at least one amylase preparation. An independent claim is also included for machine dishwashing method, comprising using the above machine dishwashing detergent.

PRODUKT UND VERFAHREN ZUM MODIFIZIEREN VON OBERFLÄCHEN UND/ODER FARBEN VON TEXTIL-ARTIKELN

PHENOL OXYDIERENDE ENZYME UND DEREN VERWENDUNG

ENDOGLUCANASE-ENZYM UND CELLULASE-ZUSAMMENSETZUNGEN, DIE DIESES ENTHALTEN

Beta-Ketoester

ALKALISCHES, LIPOLYTISCHES ENZYM

WASCHEMITTELZUSAMMENSETZUNGEN MIT PROTEASEN UND VERBESSERTEN AMYLASEN

Water free bleaching agent (containing liquid wash or cleaning agent), useful for bleaching the textiles, comprises a particle form bleaching active agent on peroxygen basis and at least an oxidation sensitive component

Water free bleaching agent (I) (containing liquid wash or cleaning agent) comprises a particle form bleaching active agent on per oxygen basis and at least a oxidation sensitive component, where the bleaching active agent or the oxidation sensitive component exists in solid matrix particle form.

Verfahren zur Reinigung von Melkanlagen

According to the inventive method for cleaning milking equipment, at least part of the aqueous solution used for cleaning is collected after the equipment has been cleaned so that it can be re-used for cleaning after the equipment has been re-used. The method is characterised in that a solution with an acidic pH is used for cleaning and in that no alkaline cleaning solution is used in addition to this acidic cleaning solution. The use of an acidic cleaning solution instead of an alkaline cleaning solution reliably ensures that undesired deposits are eliminated, especially in problem areas.

Verwendung von Polyoxyalkylenaminen in enzymhaltigen Wasch- oder Reinigungsmitteln zur Erhöhung der Stabilität von Enzymen

Die Erfindung betrifft die Verwendung von Polyoxyalkylenaminen in enzymhaltigen Wasch- oder Reinigungsmitteln zur Erhöhung der Stabilität von Enzymen sowie ein enzymhaltiges Wasch- oder Reinigungsmittel, insbesondere ein flüssiges Wasch- oder Reinigungsmittel mit verbesserter Enzymstabilität.

Grease removal, especially from drain e.g. at slaughterhouse or meat or fish processing, uses grease remover formed in situ by mixing water and dry concentrate, preferably of enzymes and bacteria

In a method of removing grease, preferably with enzymes and bacteria in aqueous form, especially for cleaning drains, with or without grease traps, the grease remover is formed in situ by combining dry concentrate and water.

Flüssige Tensidzusammensetzung mit spezieller Tensidkombination und Enzym

Flüssige Tensidzusammensetzungen, enthaltend bezogen auf das Gesamtgewicht der Zusammensetzung a) eine Gesamtmenge von 2,0 bis 8,5 Gew.-% C9-C20-Alkylbenzolsulfonat, und b) eine Gesamtmenge von 10,0 bis 18,0 Gew.-% R1-O-(CH2CH2O)n-SO3M worin R1 für eine C12-18-Alkylgruppe steht, n für eine Zahl von 2 bis 3 steht und M für ein einwertiges Kation steht, und c) eine Gesamtmenge von 1,0 bis 6,0 Gew.-% R2-O-(CH2CH2O)m-SO3M' worin R2 für eine C12-18-Alkylgruppe steht, m für eine Zahl von 7 bis 8 steht und M für ein einwertiges Kation steht, und d) eine Gesamtmenge von 2,0 bis 10,0 Gew.-% nichtionisches Tensid, und e) Wasser, und f) mindestens ein Enzym, besitzen eine für den Verbraucher akzeptable Rheologie, sind lagerstabil und ideal zur Stabilisierung von Enzymen, wie insbesondere Proteasen, geeignet.

WASCHLAUGE ZUM WASCHEN BEI NIEDRIGER TEMPERATUR UND ZUR REINIGUNG VON EIWEISSVERSCHMUTZUNGEN

ALPHA-AMYLASE-VARIANTEN

VERFAHREN ZUM GESCHIRRSPÜLEN

Verfahren zur Reinigung von Milcherhitzern

According to the invention, the surfaces of the milk heater which are to be cleaned are treated in succession with a) the aqueous solution of an acid and b) the aqueous solution of an enzyme from the group of highly alkaline proteases and then rinsed with water. The inventive method thoroughly removes the coatings left on the surfaces despite not using a strong alkali.

Biological cleaning composition for waste removal systems, e.g., pipes, which has good storage stability, includes microencapsulated microorganisms and a combination of nutrients

Spores of an aerobic, spore-forming microorganism, which are encapsulated in water-soluble microcapsules, are used in a cleaning composition for waste removal systems. The composition also contains fatty acids and derivatives of these. Cleaning composition for waste removal systems comprises: (a) a mixture of (i) glycerides of natural 1-18C fatty acids, (ii) natural 1-18C fatty acids and (iii) salts and amides of 1-18C fatty acids; and (b) spores of an aerobic, spore-forming microorganism which expresses membrane-bound lipase. The spores of the microorganism are contained, together with a carrier, in water-soluble microcapsules.

METHODEN ZUR VORBEHANDLUNG VON SCHUHEN

Verpackung für Waschmittel

MUTIERTE TRICHODERMA REESEI EGIII CELLULASEN, DAFÜR KODIERENDE DNA UND VERFAHREN ZU DEREN HERSTELLUNG

VERFAHREN ZUR BEHANDLUNG VON POLYESTERGEWEBEN

Alkalische Protease

Verfahren zur Reinigung von Geschirr in Haushalts-Geschirrspuelmaschinen sowie Mittel zur Durchfuehrung des Verfahrens

Neue Alkalische Protease aus Bacillus gibsonii und Wasch- und Reinigungsmittel enthaltend diese neue Alkalische Protease

Die vorliegende Erfindung betrifft eine neue alkalische Protease vom Subtilisin-Typ aus Bacillus gibsonii sowie hinreichend verwandte Proteine und deren Derivate. Sie betrifft außerdem Wasch- und Reinigungsmittel mit dieser neuen alkalischen Protease vom Subtilisin-Typ, hinreichend verwandten Proteinen und deren Derivaten, entsprechende Wasch- und Reinigungsverfahren und deren Verwendung in Wasch- und Reinigungsmitteln sowie weitere technische Einsatzmöglichkeiten.

Neue Amylasen

Verfahren zum gleichzeitigen Entschlichten und "Stone-Washing" von gefärbtem Denim

VERFAHREN ZUR REINIGUNG VON EINRICHTUNGEN ZUR HERSTELLUNG ODER VERARBEITUNG VON MILCHPRODUKTEN

Waschmittel sowie Verfahren zur Herstellung desselben

Protease Comprising One Or More Combinable Mutations

The present invention provides engineered protease variants. In particular, the protease variants comprise combinable mutations at selected surface positions that affect the charge and/or hydrophobicity of the enzyme to enhance at least one desired property of the resulting variant enzyme in a chosen application. Compositions comprising the protease variants, and methods for using the same are also provided.

Protease Variants

The present invention relates to protease variants. The present invention also relates to polynucleotides encoding the variant protease variants and to nucleic acid constructs, vectors, and host cells comprising the polynucleotides, and methods of using the variant enzymes, such as, in laundry and detergent compositions.

Alpha-Amylase Variants

The invention relates to a variant of a parent Termamyl-like alpha-amylase, comprising mutations in two, three, four, five or six regions/positions. The variants have increased stability at high temperatures (relative to the parent). The invention also relates to a DNA construct comprising a DNA sequence encoding an alpha-amylase variant of the invention, a recombinant expression vector which carries a DNA construct of the invention, a cell which is transformed with a DNA construct of the invention, the use of an alpha-amylase variant of the invention for washing and/or dishwashing, textile desizing, starch liquefaction, a detergent additive comprising an alpha-amylase variant of the invention, a manual or automatic dishwashing detergent composition comprising an alpha-amylase variant of the invention, a method for generating a variant of a parent Termamyl-like alpha-amylase, which variant exhibits increased.

Alpha-Amylase Mutants

The invention relates to a novel Termamyl-like alpha-amylase, and Termamyl-like alpha-amylases comprising mutations in two, three, four, five or six regions/positions. The variants have increased thermostability at acidic pH and/or at low Ca 2+ concentrations (relative to the parent). The invention also relates to a DNA construct comprising a DNA sequence encoding an alpha-amylase variant of the invention, a recombinant expression vector which carries a DNA construct of the invention, a cell which is transformed with a DNA construct of the invention, the use of an alpha-amylase variant of the invention for washing and/or dishwashing, textile desizing, starch liquefaction, a detergent additive comprising an alpha-amylase variant of the invention, a manual or automatic dishwashing detergent composition comprising an alpha-amylase variant of the invention, a method for generating a variant of a parent Termamyl-like alpha-amylase, which variant exhibits increased thermostability at acidic pH and/or at low Ca 2+ concentrations (relative to the parent).

Savinase Variants Having An Improved Wash Performance on Egg Stains

Subtilase variants having an improved wash performance on egg stains. These subtilases are useful exhibiting excellent or improved wash performance on egg stains when used in e.g. cleaning or detergent compositions, such as laundry detergent compositions and dish wash compositions, including automatic dish wash compositions.

STORAGE-STABLE LIQUID DETERGENT OR CLEANING AGENT CONTAINING PROTEASE AND LIPASE

The object is to improve the storage stability of a liquid washing or cleaning agent comprising a protease and lipase with regard to lipolytic activity. This is achieved through the use of a protease comprising an amino acid sequence that is at least 80% identical to the amino acid sequence set out in SEQ ID NO. 1 and that has the amino acid glutamic acid (E) or aspartic acid (D) or the amino acid asparagine (N) or glutamine (Q) or the amino acid alanine (A) or glycine (G) or serine (S) at position 99 in the sequence corresponding to SEQ ID NO. 1. 1. A liquid washing or cleaning agent comprising: i) a protease comprising an amino acid sequence that is at least 80% identical to the amino acid sequence set out in SEQ ID NO. 1 and that has the amino acid glutamic acid (E) or aspartic acid (D) at position 99 in the sequence corresponding to SEQ ID NO. 1;', 'ii) a protease comprising an amino acid sequence that is at least 80% identical to the amino acid sequence set out in SEQ ID NO. 1 and that has the amino acid asparagine (N) or glutamine (Q) at position 99 in the sequence corresponding to SEQ ID NO. 1;', 'iii) a protease comprising an amino acid sequence that is at least 80% identical to the amino acid sequence set out in SEQ ID NO. 1 and that has the amino acid alanine (A) or glycine (G) or serine (S) at position 99 in the sequence corresponding to SEQ ID NO. 1;, '(a) a protease selected from the group of proteases consisting of(b) a lipase.2. The washing or cleaning agent according to claim 1 , wherein the protease additionally has at least one of the following amino acids in the sequence corresponding to SEQ ID NO. 1:(a) threonine at position 3 (3T),(b) isoleucine at position 4 (4I),(c) alanine, threonine or arginine at position 61 (61A, 61T or 61R),(d) aspartic acid or glutamic acid at position 154 (154D or 154E),(e) proline at position 188 (188P),(f) methionine at position 193 (193M),(g) isoleucine at position 199 (199I),(h) aspartic acid, glutamic acid or ...

USE OF AMYLASE VARIANTS AT LOW TEMPERATURE

The present invention relates to the use of alpha-amylase variants having improved activity relative to the parent enzyme at low temperature, including improved washing and/or dishwashing performance and/or increased stability at low temperature. The invention further relates a method for doing laundry, dish wash and/or cleaning such as institutional cleaning and to compositions for use at low temperature. 1. Use in a starch removing process of a variant or a variant of a parent alpha-amylase , wherein said variant comprises a deletion at one or more positions corresponding to positions selected from the group consisting of 180 , 181 , 182 , 183 and 184 of the mature polypeptide of SEQ ID NO 3 , wherein said variant having at least one improved property compared to an alpha-amylase having the identical amino acid sequence of said variant but not having the deletion at one or more of said positions , or compared to the parent alpha-amylase or compared to an alpha-amylase having the amino acid sequence shown in SEQ ID NO 4 and wherein the temperature in the starch removing process is below 40 deg C. , such as below 35 deg C.2. Use in laundry , dish wash , industrial or institutional cleaning of a variant or a variant of a parent alpha amylase , comprising a deletion at one or more positions corresponding to positions selected from the group comprising 180 , 181 , 182 , 183 and 184 of the mature polypeptide of SEQ ID NO 3 , wherein said variant having at least one improved property compared to an alpha-amylase having the identical amino acid sequence of said variant but not having the deletion at one or more of said positions , or compared to the parent alpha amylase or compared to SEQ ID NO 4 and wherein the temperature in laundry , dish wash , industrial and institutional cleaning is below 40 deg C. , such as below 35 deg C.3. The use according to claim 1 , wherein the starch removing process or the cleaning process is performed at temperature below 32 deg C. claim 1 ...

Polypeptides Having Cellobiohydrolase 1 Activity and Polynucleotides Encoding Same

The present invention relates to polypeptides having cellobiohydrolase I activity and polynucleotides having a nucleotide sequence which encodes for the polypeptides. The invention also relates to nucleic acid constructs, vectors, and host cells comprising the nucleic acid constructs as well as methods for producing and using the polypeptides. 129-. (canceled)30. An isolated polypeptide having cellobiohydrolase I activity , which has at least 80% identity with the sequence of amino acids 1 to 529 of SEQ ID NO:4.31. The polypeptide of claim 30 , which has at least 85% identity with amino acids 1 to 529 of SEQ ID NO:4.32. The polypeptide of claim 30 , which has at least 90% identity with amino acids 1 to 529 of SEQ ID NO:4.33. The polypeptide of claim 30 , which has at least 95% identity with amino acids 1 to 529 of SEQ ID NO:4.34. The polypeptide of claim 30 , which has at least 97% identity with amino acids 1 to 529 of SEQ ID NO:4.35. The polypeptide of claim 30 , which has at least 98% identity with amino acids 1 to 529 of SEQ ID NO:4.36. The polypeptide of claim 30 , which has at least 99% identity with amino acids 1 to 529 of SEQ ID NO:4.37. The polypeptide of claim 30 , comprising the sequence of amino acids 1 to 529 of SEQ ID NO:4.38. The polypeptide of claim 30 , which is a fragment of the sequence of amino acids 1 to 529 of SEQ ID NO:4.39. A detergent composition comprising a surfactant and the polypeptide of .40. A method for producing ethanol from biomass claim 30 , comprising{'claim-ref': {'@idref': 'CLM-00030', 'claim 30'}, '(a) contacting the biomass with the polypeptide of , an endo-1,4-beta-glucanase, and a beta-D-glucosidase to produce sugar; and'}(b) fermenting the sugar to produce ethanol. This application is a divisional of U.S. application Ser. No. 13/646,980 filed on Oct. 8, 2012, now pending, which is a divisional of U.S. application Ser. No. 13/483,389 filed on May 30, 2012, now pending, which is a divisional of U.S. application Ser. No. 12/818 ...

LOW AND HIGH TEMPERATURE ENZYMATIC SYSTEM

An enzymatic system includes a first pH neutral composition and a second pH neutral composition. The first pH neutral composition includes a low temperature enzyme effective at removing blood and hemoglobin. The second pH neutral composition includes a high temperature enzyme effective at removing mucous, fibrin and fat. In one embodiment, the low temperature enzyme has an activation temperature of about 50 degrees to about 120 degrees Fahrenheit and the high temperature enzyme has an activation temperature of about 140 to about 180 degrees Fahrenheit. 1. A method of cleaning a surgical instrument comprising: a. about 5 weight % to about 20 weight % of a low temperature enzyme, the low temperature enzyme consisting of a lipase or a protease or a combination thereof,', 'b. a water soluble calcium salt as a stabilizing agent,', 'c. at least 17.5 weight % filler comprised of sodium gluconate and sodium sulfate,', 'd. a hardening agent comprised of polyethylene glycol, and', 'e. sodium citrate;, '(a) contacting the surgical instrument with water having a temperature of about 50 degrees to about 120 degrees Fahrenheit with a first enzymatic composition, the first enzymatic composition, comprising(b) removing the first enzymatic composition from the surgical instrument; a. about 5 weight % to about 20 weight % of a high temperature enzyme, the high temperature enzyme consisting of a lipase or a protease or a combination thereof,', 'b. a water soluble calcium salt as a stabilizing agent;', 'c. a filler comprised of sodium gluconate and sodium sulfate,', 'd. a hardening agent comprised of polyethylene glycol, and', 'e. sodium citrate; and, '(c) washing the surgical instrument in water having a temperature of about 140 to about 180 degrees Fahrenheit and a second enzymatic composition comprising, the second enzymatic composition, comprising(d) rinsing the surgical instrument.2. The method of claim 1 , wherein contacting the surgical instrument comprises immersing the ...

Concentrated Soak Wash

The present invention relates to a method for cleaning an object comprising the steps: (a) distributing to the object a first soak solution comprising at least one surfactant and at least one enzyme followed by a first soak period wherein the concentrations of the at least one surfactant and the at least one enzyme are higher relative to their concentrations in a subsequent wash solution; (b) furthermore adding to the object water to obtain a wash solution followed by a wash period; and (c) rinsing the object; wherein said method has a wash performance corresponding to any of (i) a Relative Wash Performance (RWP) of at least 1; (ii) a Process Related Cleaning Index (PRCI) of more than 1; or (iii) a Relative Wash Performance (RWP) of at least 1 and a Process Related Cleaning Index (PRCI) of more than 1. 115-. (canceled)16. A method for cleaning an object comprising the steps:(a) distributing to the object a first soak solution comprising at least one surfactant and at least one enzyme followed by a first soak period wherein the concentrations of the at least one surfactant and the at least one enzyme are higher relative to their concentrations in a subsequent wash solution;(b) furthermore adding to the object water to obtain a wash solution followed by a wash period; and(c) rinsing the object;wherein said method has a wash performance corresponding to any of (i) a Relative Wash Performance (RWP) of at least 1; (ii) a Process Related Cleaning Index (PRCI) of more than 1; or (iii) a Relative Wash Performance (RWP) of at least 1 and a Process Related Cleaning Index (PRCI) of more than 1.17. The method of claim 16 , wherein no agitation or other mechanical action is applied during the soak period after the initial agitation for the purpose of distributing the soak solution to and wetting of the object.18. The method of claim 16 , wherein agitation or other mechanical action is applied during the wash period.19. The method of claim 16 , wherein the concentration of the at ...

Novel whitening agents for cellulosic substrates

This invention relates to novel whitening agents for cellulosic substrates. The whitening agents are comprised of at least two components: at least one chromophore component and at least one polymeric component. Suitable chromophore components generally fluoresce blue, red, violet, or purple color when exposed to ultraviolet light, or they may absorb light to reflect these same shades. The whitening agents are further characterized by having a dispersion component value of the Hansen Solubility Parameter of less than or equal to about 17 MPa 0.5 . This invention also relates to laundry care compositions including but not limited to liquid and/or powder laundry detergent formulations and rinse added fabric softening (RAFS) compositions that comprise such whitening agents.

Eubacterial RNA-Polymerase Mutants With Altered Product Production

The present invention relates to an isolated mutant comprising at least one mutation resulting in a substitution of at least one amino acid in the beta-subunit of the RNA-polymerase encoded for by the rpoB-gene providing an altered production of a product of interest when said production of a product of interest is compared to the production of the same product in an isogenic wild type strain grown at identical conditions, wherein the substitution of at least one amino acid occurs at any of positions 469, 478, 482, 485, or 487 of SEQ ID NO:2, or at the equivalent positions in any eubacterial RNA-polymererase beta-subunit family member. Another aspect of the invention relates to a process for producing at least one product of interest in a mutant and to a use of the mutant according to the invention for producing at least one product of interest. 1eubacterium. An isolated mutant comprising at least one mutation resulting in a substitution of at least one amino acid in the beta-subunit of the RNA-polymerase encoded for by the rpoB-gene providing an altered production of a product of interest when said production of a product of interest is compared to the production of the same product in the isogenic parent strain grown at identical conditions , wherein the substitution of at least one amino acid occurs at any of positions 469 , 478 , 482 , 485 , or 487 in SEQ ID NO:2 , or at the equivalent positions in any eubacterial RNA-polymerase beta-subunit family member.2eubacterium. The isolated mutant of claim 1 , wherein the substitution of at least one amino acid provides an improved production of the product of interest claim 1 , or a higher yield of the product of interest.3eubacterium. The isolated mutant of claim 1 , wherein the substitution of at least one amino acid comprises Q469R claim 1 , A478D claim 1 , A478V claim 1 , H482R claim 1 , H482P claim 1 , R485H claim 1 , or S487L.4eubacterium. The isolated mutant of claim 1 , wherein the substitution of at least one ...

Subtilases

The present invention relates to methods for producing variants of a parent TY145 subtilase and of a parent BPN′ subtilase and to TY145 and BPN′ variants having altered properties as compared to the parent TY145/BPN′ subtilase. 1. A TY145 like subtilase variant which is at least 63% homologous to the sequence of SEQ ID NO:1 , which variant comprises: a) the Weak ion-binding site are: 154, 155, 158, 164, 165, 166, 167, 168, 178, 179, 180, 181, 182, 183, 184, 185, 186, 187, 188, 189, 190, 191, 211, 220, 221, 222, 223, 224, 225, 226, 227, 228, 277, 281 and 305,', 'b) the Near ion-binding site are: 185, 211, 212, 213, 214, 215, 216, 217, 218, 219, 220, 221, 222, 223, 224, 225, 226, 227, 277, 281, 299, 300, 301, 304, 305,', 'c) the Far ion-binding site are: 193, 198, 199, 201, 202, 204, 216, 217, 219, 226, 227, 228, 229, 284, 285, 286, 287, 288, 289, 290, 291, 292, 293, 294, 295, 296, 297, 298, 299, 300, 301, 302, 303, 304, 305, 306 and 307;, '(1) an alteration in one or more positions located at a distance of not more than 10 Å to one of the ion-binding sites of TY145, wherein the positions, as specified in SEQ ID NO:1, located at a distance of not more than 10 Å to 84, 85, 86, 87 and 88,', '108, 109, 110, 111, 112, 113, 114, 115, 116 and 117,', '141, 142, 143, 144, 145 and 146,', '150, 151 and 152,', '169, 170 and 171,', '200 and 201,', '211, 212, 213, 214, 215, 216, 217, 218, 219 and 220,', '242 and 243, 268, 269 and 270;, '(2) one or more alterations in one or more of the positions contained in the following highly mobile regions 1, 2, 3, 4, 5, 6 and 7,', '17, 18, 19, 20, 21, 22 and 23,', '38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, 49 and 50,', '57, 58, 59, 60, 61, 62, 63, 64, 65, 66, 67, 68 and 69,', '84, 85, 86, 87, 88, 89, 90, 91 and 92,', '107, 108, 109 and 110,', '239, 240, 241, 242 and 243', '265 and 266,', 'wherein said alterations preferably are introduced in one or both of the regions 57-69 and 84-92;, '(3) one or more alterations in one or more of the ...

CONSUMER PRODUCTS

This invention relates to consumer products comprising proteases, particularly cold water proteases and processes for making and using such products. Such consumer products provide improved cleaning, whiteness and/or freshness. Such proteases are derived from a parent enzyme, for example , by substitution, insertion and/or deletion of one or more of the parent enzymes' amino acids. 1. A composition comprising an adjunct material and a cold water protease variant , said composition being a consumer product.2. A composition according to wherein the protease variant has a performance index of at least 1.1 claim 1 , at least 1.2 claim 1 , at least 1.3 claim 1 , at least 1.4 claim 1 , at least 1.5 claim 1 , at least 1.6 claim 1 , at least 1.7 claim 1 , at least 1.8 claim 1 , at least 1.9 claim 1 , at least 2; from 1.1 to about 10 claim 1 , from 1.1 to about 8 or even from 1.1 to about 5 according to Test Method 6.3Bacillus lentusBacillus amyloliquefaciens. A composition comprising an adjunct material and a protease variant claim 1 , wherein said protease variant comprises one or more of the following sets of mutations: G020R-N043R claim 1 , N062E-A158E claim 1 , S103G-A158E claim 1 , S128N-A158E claim 1 , A016S-A158E claim 1 , V104L-A158E claim 1 , E089P-A158E claim 1 , L111V-A158E claim 1 , T022A-A158E claim 1 , S101A-A158E claim 1 , L148I-A158E claim 1 , P129E-A158E claim 1 , T022A-E089P claim 1 , A016S-E089P claim 1 , N062E-E089P claim 1 , N062E-E271F claim 1 , A158E-E271F claim 1 , R186H-E271F claim 1 , P129E-E271F claim 1 , L111V-E271F claim 1 , Y209E-E271F claim 1 , A016S-E271F claim 1 , S188D-E271F claim 1 , T022A-E271F claim 1 , G159E-E271F claim 1 , V104L-E271F claim 1 , S101A-E271F claim 1 , E089P-E271F claim 1 , S128N-E271F claim 1 , S103G-E271F claim 1 , L148I-E271F claim 1 , H249R-E271F claim 1 , N062E-G159E claim 1 , A016S-G159E claim 1 , S128N-G159E claim 1 , L148I-G159E claim 1 , L111V-G159E claim 1 , E089P-G159E claim 1 , T022A-G159E claim 1 , P129E- ...

Machine Dishwashing Compositions and Methods

A machine dishwashing main-wash detergent composition or a dishwashing machine cleaning composition comprising at least one cellulase enzyme, and at least one pectinase enzyme is provided. The compositions optionally also comprise at least one lipase, surfactant (especially non-ionic surfactant) and a pH buffering system. 1. (canceled)2. (canceled)3. (canceled)4. (canceled)5. (canceled)6. (canceled)7. (canceled)8. (canceled)9. (canceled)10. (canceled)11. (canceled)12. (canceled)13. (canceled)14. A machine dishwashing main-wash detergent composition or a dishwashing machine cleaning composition comprising;(i) at least one cellulase enzyme, and(ii) at least one pectinase enzyme.15. A composition according to claim 14 , wherein the at least one cellulase enzyme is present in an amount of from 0.005 wt % to 2.5 wt % of active enzyme based on the total weight of the composition16. A composition according to wherein the at least one pectinase enzyme is present in an amount of from 0.005 wt % to 2.5 wt % of active enzyme based on the total weight of the composition.17. A composition according to claim 14 , wherein the composition further comprises at least one enzyme selected from lipases and proteases.16. A composition according to claim 17 , wherein the composition comprises an active amount of the at least one lipase and/or protease in the range of from 0.005 wt % to 2.5 wt % of active enzyme based on the total weight of the composition.17. A composition according to claim 14 , wherein the composition further comprises 0.1 to 10 wt % alkoxylated non-ionic surfactant based on the total weight of the composition.18. A composition according to claim 14 , wherein the composition is a machine cleaner composition and has an acidic pH.19. A composition according to claim 18 , wherein the composition is a machine cleaner composition having a pH of between 3 and 6.20. A composition according to claim 14 , wherein the composition is a machine cleaner composition and further ...

Multiply-Substituted Protease Variants

Novel protease variants derived from the DNA sequences of naturally-occurring or recombinant non-human proteases are disclosed. The variant proteases, in general, are obtained by in vitro modification of a precursor DNA sequence encoding the naturally-occurring or recombinant protease to generate the substitution of a plurality of amino acid residues in the amino acid sequence of a precursor protease. Such variant proteases have properties which are different from those of the precursor protease, such as altered wash performance. The substituted amino acid residue equivalent to positions 7, 23, 26, 28, 29, 30, 31, 47, 66, 69, 73, 82, 85, 88, 90, 92, 93, 105, 113, 139, 148, 149, 150, 151, 178, 200, 201, 231, 233, 267 and/or 273 of Bacillus amyloliquefaciens subtilisin.

Multiply-Substituted Protease Variants

Novel enzyme variants including protease variants derived from the DNA sequences of naturally-occurring or recombinant non-human proteases are disclosed. The variant proteases, in general, are obtained by in vitro modification of a precursor DNA sequence encoding the naturally-occurring or recombinant protease to generate the substitution of a plurality of amino acid residues in the amino acid sequence of a precursor protease. Such variant proteases have properties which are different from those of the precursor protease, such as altered wash performance. The substituted amino acid residue correspond to positions 27, 45, 170, 181, 251 and 271 of subtilisin. Additional variants comprising at least one additional substitution at a position selected from 1, 14, 49, 61, 87, 100, 102, 118, 128, 204 and 258 of subtilisin are also described. 1. A protease variant of a precursor protease , said variant comprising one or more modifications at a charged amino acid residue position , said variant being characterized by having the same net electrostatic charge as said precursor protease.2. The protease variant of claim 1 , wherein said charged amino acid residue position is selected from the group consisting of aspartic acid claim 1 , glutamic acid claim 1 , lysine and arginine.3Bacillus amyloliquefaciens. The protease variant of claim 1 , wherein said variant comprises an amino acid sequence having a substitution at one or more residue positions equivalent to residue positions selected from the group consisting of 27 claim 1 , 45 claim 1 , 170 claim 1 , 181 claim 1 , 251 and 271 of subtilisin as set forth in SEQ ID NO. 2.4. The protease variant of claim 3 , wherein said variant comprising a substitution at one or more positions corresponding to 27 claim 3 , 45 claim 3 , 170 claim 3 , 181 claim 3 , 251 and 271 is a substitution selected from K27T claim 3 , R45N claim 3 , R170S claim 3 , D181N claim 3 , K251G and E271T.5Bacillus amyloliquefaciens. The protease variant of claim 3 ...

PROTEASES PRODUCING AN ALTERED IMMUNOGENIC RESPONSE AND METHODS OF MAKING AND USING THE SAME

The present invention provides novel protein variants that exhibit reduced immunogenic responses, as compared to the parental proteins. The present invention further provides DNA molecules that encode novel variants, host cells comprising DNA encoding novel variants, as well as methods for making proteins less allergenic. In addition, the present invention provides various compositions that comprise these proteins that are less immunogenic than the wild-type proteins. 1Bacillus amyloliquefaciens. A variant of a protease of interest comprising a T-cell epitope , wherein said variant differs from said protease of interest by having an altered T-cell epitope such that said variant exhibits an altered immunogenic response from said protease of interest in a human; wherein said altered T-cell epitope of said protease of interest includes one or more amino acid substitutions at residues corresponding to 88 , 89 , 90 , 93 , 98 , 99 , 100 , 102 , 154 , 155 , 156 , 157 , 158 , 160 , 161 , 162 , 163 , 166 , 168 , 169 , 173 , 174 , 175 , 176 , 177 , 181 , 182 , 183 , 184 , 185 , 186 , 187 , and 188 of subtilisin.2. The variant of wherein said immunogenic response produced by said variant is less than said immunogenic response produced by said protease of interest.3. The variant of claim 2 , wherein said immunogenic response produced by said variant is characterized by an in vivo reduction in allergenicity.4. The variant of claim 2 , wherein said immunogenic response produced by said variant is characterized by an in vitro reduction in allergenicity.5. The variant of wherein said immunogenic response produced by said variant is greater than said immunogenic response produced by said protease of interest.6. A nucleic acid encoding the variant of .7. An expression vector comprising the nucleic acid of .8. A host cell transformed with the expression vector of .9. A composition selection from the group consisting of cleaning compositions claim 1 , and personal care products claim 1 ...

Dish Detergent Comprising Bleaching Enzymes

Described are compositions and methods that involve using bleaching enzymes in dish detergents. In some preferred embodiments, the bleaching enzyme comprises at least one laccase, while in some alternative preferred embodiments, the bleaching enzyme comprises at least one glucose oxidase suitable for use in dish detergents. In some additional preferred embodiments, the dish detergents are machine dish detergents.

Subtilase Variants

The present invention relates to novel subtilase variants exhibiting alterations relative to the parent subtilase in one or more properties including: Wash performance, thermal stability, storage stability or catalytic activity. The variants of the invention are suitable for use in e.g. cleaning or detergent compositions, such as laundry detergent compositions and dishwash compositions, including automatic dishwash compositions. 1. A subtilase variant comprising at least one or more of the following alterations:X11{A,R,N,D,C,Q,E,G,H,I,L,K,M,F,S,T,W,Y,V}, deletion, insertion;X30{A,R,N,D,C,Q,E,G,H,I,L,K,M,F,P,S,T,W,Y,V}, deletion, insertion;X31{R,N,D,Q,E,H,K,M,P,W,Y}, deletion, insertion;X32{A,R,D,C,E,G,H,I,L,K,M,F,P,T,W,Y,V}, insertion;X34{A,R,N,D,C,Q,E,G,H,I,L,K,M,F,S,T,W,Y,V}, deletion;X65{A,R,C,G,H,I,L,K,M,F,T,W,Y,V}, deletion, insertion;X66{A,R,C,H,I,L,K,M,F,T,W,Y,V}, deletion, insertion;X67{A,R,N,Q,G,H,I,K,M,F,P,S,T,W,Y,V};X68{R,N,D,Q,E,G,H,I,L,K,F,P,S,T,W,Y,V}, deletion, insertion;X69{A,R,N,D,Q,E,G,H,I,L,K,M,F,P,S,T,W,Y,V}, deletion, insertion;X70G;X71T;X77N;X83G, insertion;X84V;X85{A,R,N,D,Q,E,G,H,I,L,M,F,S,T,W,Y,V};X90{A,R,N,D,C,Q,E,G,H,I,L,K,M,F,P,S,T,W,Y,V}, deletion, insertion;X95{R,K,F,W,Y,V}, deletion;X107IX110G, insertion;X121V, insertion;X122 insertion;X123N;X125S;X150{A,R,N,D,Q,E,G,H,I,L,K,M,F,P,S,T,W,Y,V}, deletion, insertion;X152{A,R,N,D,Q,E,H,K,F,P,W,Y,V};X153{R,N,D,Q,E,G,H,I,L,K,M,F,T,W,Y,V};X154{A,R,G,H,I,L,M,F,W,Y,V};X164{A,R,H,T,W};X165{R,L,F,W,Y};X166{W,Y}, insertion;X175{R,N,D,Q,E,G,H,K,M,F,P,T,W,Y,V};X177{R,N,D,Q,E,G,H,I,L,K,M,F,P,S,T,W,Y,V}, deletion, insertion;X178{A,R,N,D,C,Q,E,G,H,I,L,K,M,F,P,S,T,W,Y,V}, deletion, insertion;X180{A,R,N,D,C,Q,E,G,H,I,L,K,M,F,P,S,T,W,Y,V}, deletion, insertion;X199{R,L,K,F,W,Y,V}, deletion, insertion;X200{A,R,I,L,K,M,F,W,Y,V}, deletion, insertion;X201{A,R,H,I,L,K,M,F,P,T,W,Y,V}, deletion, insertion;X202{A,R,C,G,H,I,L,K,M,F,T,W,Y,V};X207{A,R,N,C,Q,G,H,I,L,K,M,F,P,S,T,W,Y,V};X220T, insertion;X223A, insertion; ...

COMPOSITIONS AND METHODS COMPRISING SERINE PROTEASE VARIANTS (AS AMENDED)

The present invention provides serine protease variants produced there from. Specifically, the present invention provides serine protease variants having one or more substitutions as compared to a reference serine protease. In addition, the present invention provides compositions comprising these serine protease variants. In some embodiments, the present invention provides cleaning compositions comprising at least one of these serine protease variants. 1Bacillus lentusBacillus amyloliquefaciens. An isolated subtilisin variant , wherein said subtilisin variant is a mature form having proteolytic activity and comprises an amino acid sequence comprising a combination of amino acid substitutions selected from: T022A-E271F , G020R-N043R , N062E-A158E , S103G-A158E , S128N-A158E , A016S-A158E , V104L-A158E , E089P-A158E , L111V-A158E , T022A-A158E , S101A-A158E , L148I-A158E , P129E-A158E , T022A-E089P , A016S-E089P , N062E-E089P , N062E-E271F , A158E-E271F , R186H-E271F , P129E-E271F , L111V-E271F , Y209E-E271F , A016S-E271F , S188D-E271F , G159E-E271F , V104L-E271F , S101A-E271F , E089P-E271F , S128N-E271F , S103G-E271F , L148I-E271F , H249R-E271F , N062E-G159E , A016S-G159E , S128N-G159E , L148I-G159E , L111V-G159E , E089P-G159E , T022A-G159E , P129E-G159E , S103G-G159E , V104L-G159E , A158E-G159E , S101A-G159E , A158E-H249R , L111V-H249R , P129E-H249R , N062E-H249R , A016S-H249R , R186H-H249R , L148I-H249R , G159E-H249R , S101A-H249R , S188D-H249R , V104L-H249R , Y209E-H249R , T022A-H249R , S128N-H249R , S103G-H249R , E089P-H249R , T022A-L111V , S101A-L111V , A016S-L111V , V104L-L111V , N062E-L111V , S103G-L111V , E089P-L111V , A016S-L148I , N062E-L148I , T022A-L148I , P129E-L148I , V104L-L148I , S103G-L148I , S128N-L148I , S101A-L148I , E089P-L148I , L111V-L148I , A016S-N062E , T022A-N062E , N062E-P129E , T022A-P129E , S128N-P129E , A016S-P129E , S101A-P129E , V104L-P129E , E089P-P129E , S103G-P129E , L111V-P129E , N062E-R186H , S128N-R186H , S101A-R186H , T022A- ...

Protease Variants Active over a Broad Temperature Range

The present invention provides protease compositions particularly suited for dishwashing applications. 18-. (canceled)9. An isolated nucleic acid encoding a modified subtilisin as set forth in .10. A vector comprising the isolated nucleic acid of .11. A host cell comprising the vector of .12. A dishwashing method claim 13 , comprising the steps of: providing at least one modified subtilisin as set forth in and dishware in need of cleaning; and contacting said dishware with said modified subtilisin under conditions effective to provide cleaning of said dishware.13. A dishwashing composition comprising a modified subtilisin claim 13 , wherein said subtilisin has at least 70% homology with the sequence of mature PB92 serine protease of SEQ ID NO: 2 claim 13 , and comprises substitution G116V.14. The dishwashing composition of claim 13 , wherein said modified subtilisin comprises substitutions made at positions G116 claim 13 , S126 claim 13 , P127 claim 13 , and S128.15. The dishwashing composition of claim 13 , wherein said subtilisin comprises the substitution G116V and the additional mutation is selected from the group consisting of S128F claim 13 , S128L claim 13 , S128N claim 13 , S128R claim 13 , S128V claim 13 , P129E claim 13 , P129L claim 13 , P129M claim 13 , P129N claim 13 , P129L claim 13 , P129Q claim 13 , P1295 claim 13 , 5130A claim 13 , S130K claim 13 , S130P claim 13 , S130T claim 13 , S130V claim 13 , and S166D.16. The dishwashing composition of claim 13 , wherein said modified subtilisin comprises substitutions made at positions S126 claim 13 , P127 claim 13 , and S128.17. The dishwashing composition of claim 16 , wherein said substitutions are selected from the group consisting of S128C claim 16 , S128R claim 16 , P129Q claim 16 , P129R claim 16 , S130D claim 16 , and S130G.18. The dishwashing composition of claim 13 , wherein said modified subtilisin has the amino acid sequence of mature PB92 serine protease of SEQ ID NO: 2 with the substitutions: ...

Subtilases

The present invention relates to methods for producing variants of a parent TY145 subtilase and of a parent BPN′ subtilase and to TY145 and BPN′ variants having altered properties as compared to the parent TY145/BPN′ subtilase. 1. A TY145 like subtilase variant which is at least 63% homologous to the sequence of SEQ ID NO:1 , which variant comprises: a) the Weak ion-binding site are: 154, 155, 158, 164, 165, 166, 167, 168, 178, 179, 180, 181, 182, 183, 184, 185, 186, 187, 188, 189, 190, 191, 211, 220, 221, 222, 223, 224, 225, 226, 227, 228, 277, 281 and 305,', 'b) the Near ion-binding site are: 185, 211, 212, 213, 214, 215, 216, 217, 218, 219, 220, 221, 222, 223, 224, 225, 226, 227, 277, 281, 299, 300, 301, 304, 305,, '(1) an alteration in one or more positions located at a distance of not more than 10 Å to one of the ion-binding sites of TY145, wherein the positions, as specified in SEQ ID NO:1, located at a distance of not more than 10 Å toc) the Far ion-binding site are: 193, 198, 199, 201, 202, 204, 216, 217, 219, 226, 227, 228, 229, 284, 285, 286, 287, 288, 289, 290, 291, 292, 293, 294, 295, 296, 297, 298, 299, 300, 301, 302, 303, 304, 305, 306 and 307; 84, 85, 86, 87 and 88,', '108, 109, 110, 111, 112, 113, 114, 115, 116 and 117,', '141, 142, 143, 144, 145 and 146,', '150, 151 and 152,', '169, 170 and 171,', '200 and 201,', '211, 212, 213, 214, 215, 216, 217, 218, 219 and 220,', '242 and 243, 268, 269 and 270;, '(2) one or more alterations in one or more of the positions contained in the following highly mobile regions 1, 2, 3, 4, 5, 6 and 7,', '17, 18, 19, 20, 21, 22 and 23,', '38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, 49 and 50,', '57, 58, 59, 60, 61, 62, 63, 64, 65, 66, 67, 68 and 69,', '84, 85, 86, 87, 88, 89, 90, 91 and 92,', '107, 108, 109 and 110,', '239, 240, 241, 242 and 243', '265 and 266,', 'wherein said alterations preferably are introduced in one or both of the regions 57-69 and 84-92;, '(3) one or more alterations in one or more of the ...

Combining BioPolishing and Bleach Clean-up

The present invention provides methods and compositions for treating textile, wherein the textile is treated by a system for removing hydrogen peroxide and an enzyme system for bio-polishing in one step to achieve the biopolishing and bleach clean up effect. The present invention further provides a one step process to achieve biopolishing. 132-. (canceled)33. A one-step process for combined biopolishing and bleach clean up of treating textile , comprising the step of treating the textile with (i) a system for removing hydrogen peroxide , and (ii) an enzyme system for bio-polishing , wherein the system for removing hydrogen peroxide and the enzyme system for bio-polishing are added simultaneously or sequentially to a single solution containing the textile.34. The process of claim 33 , wherein the system for removing hydrogen peroxide comprises a catalase or chemical reducing agent.35. The process of claim 34 , wherein the catalase is derived from bacterial claim 34 , yeast claim 34 , fungi claim 34 , or animal.36Bacillus, PseudomonasStreptomycesCandida, Kluyveromyces, Pichia, Saccharomyces, SchizosaccharomycesYarrowiaAcremonium, Aspergillus, Aureobasidium, Bjerkandera, Ceriporiopsis, Coprinus, Coriolus, Cryptococcus, Filibasidium, Fusarium, Humicola, Magnaporthe, Micrococcus Mucor, Myceliphthora, Neocallimastix, Neurospora, Paecilomyces, Penicillium, Phanerochaete, Phlebia, Piromyces, Pleurotus, Schizophyllum, Scytalidium, Talaromyces, Thermoascus, Thielavia, Tolypocladium, TrametesTrichoderma. The process of claim 35 , wherein the catalase is derived from bacteria such as or strain; yeast such as or ; fungal such as claim 35 , or strain; or animal such as pig liver claim 35 , beef lever.37Scytalidium thermophilum. The process of claim 34 , wherein the catalase is catalase of SEQ ID NO: 3 claim 34 , or a variant thereof.38. The process of claim 33 , wherein the enzyme system for biopolishing comprises a cellulase.39Aspergillus, Bacillus, Fusarium, Geotricum, Humicola ...

ENHANCED PROTEIN EXPRESSION IN BACILLUS

The present invention provides cells that have been genetically manipulated to have an altered capacity to produce expressed proteins. In particular, the present invention relates to Gram-positive microorganisms, such as species having enhanced expression of a protein of interest, wherein one or more chromosomal genes have been inactivated, and preferably wherein one or more chromosomal genes have been deleted from the chromosome. In some further embodiments, one or more indigenous chromosomal regions have been deleted from a corresponding wild-type host chromosome. 1Bacillus. A method for enhancing expression of a protein of interest from comprising:{'i': Bacillus', 'Bacillus, 'a) obtaining an altered strain capable of producing a protein of interest, wherein said altered strain has at least one inactivated chromosomal gene selected from the group consisting of sbo, slr, ybcO, csn, spoIISA, sigB, phrC, rapA, CssS, trpA, trpB, trpC, trpD, trpE, trpF, tdh/kbl, alsD, sigD, prpC, gapB, pckA, fbp, rocA, ycgN, ycgM, rocF, and rocD; and'}{'i': Bacillus', 'Bacillus', 'Bacillus, 'b) growing said altered strain under conditions such that said protein of interest is expressed by said altered strain, wherein said expression of said protein of interest is enhanced compared to the expression of said protein of interest in an unaltered host strain.'}2. The method of claim 1 , wherein said protein of interest is selected from the group consisting of homologous proteins and heterologous proteins.3. The method of claim 1 , wherein said protein of interest is an enzyme selected from the group consisting of proteases claim 1 , cellulases claim 1 , amylases claim 1 , carbohydrases claim 1 , lipases claim 1 , isomerases claim 1 , transferases claim 1 , kinases claim 1 , and phosphatases.4. The method of claim 3 , wherein said protein of interest is a protease.5Bacillus. The method of claim 1 , wherein said altered strain is obtained by deleting one or more chromosomal genes selected ...

Protein Variants Having Modified Immunogenicity

The present invention relates to a method of selecting a protein variant having modified immunogenicity as compared to the parent protein comprising the steps obtaining antibody binding peptide sequences, using the sequences to localise epitope sequences on the 3-dimensional structure of parent protein, defining an epitope area including amino acids situated within 5 Å from the epitope amino acids constituting the epitope sequence, changing one or more of the amino acids defining the epitope area of the parent protein by genetical engineering mutations of a DNA sequence encoding the parent protein, introducing the mutated DNA sequence into a suitable host, culturing said host and expressing the protein variant, and evaluating the immunogenicity of the protein variant using the parent protein as reference. The invention further relates to the protein variant and use thereof, as well as to a method for producing said protein variant. 1134-. (canceled)135. A protease variant having modified immunogenicity as compared to a parent protease , obtainable by a method comprising the steps of:(a) obtaining antibody binding peptide sequences,(b) using the sequences to localise epitope sequences on the 3-dimensional structure of the parent protein,(c) defining an epitope area including amino acids situated within 5 Å from the epitope amino acids constituting the epitope sequence,(d) changing one or more of the amino acids defining the epitope area of the parent protein by genetic engineering mutations of a DNA sequence encoding the parent protein,(e) introducing the mutated DNA sequence into a suitable host, culturing said host and expressing the protein variant, and(f) evaluating the immunogenicity of the protein variant using the parent protein as reference.143. The savinase-like subtilisin of claim 141 , wherein the subtilisin has at least 81% homology to SEQ ID NO: 24.144. The savinase-like subtilisin of claim 141 , wherein the subtilisin has any of the amino acid sequence ...

Performance-enhanced protease variants

Proteases encompassing an amino acid sequence, which are at least 70% identical to the amino acid sequence specified in SEQ ID NO. 1 over the entire length thereof and which, in the listing according to SEQ ID NO. 1, have the amino acid substitution I21V in combination with at least one further amino acid substitution, the further amino acid substitution being selected from the group consisting of Q12L, M122L, N177V, A222S, V228I and T247N, and agents encompassing such proteases, exhibit very good cleaning performance on egg-containing stains.

STORAGE-STABLE LIQUID WASHING OR CLEANING AGENT CONTAINING PROTEASE AND AMYLASE

According to the invention, storage stability in terms of amylolytic activity is to be improved in a liquid washing or cleaning agent which comprises a protease and amylase. This is achieved by the use of a protease which comprises an amino acid sequence which is at least 80% identical to the amino acid sequence specified in SEQ ID NO. 1 and which has the amino acid glutamic acid (E) or aspartic acid (D) or the amino acid asparagine (N) or glutamine (Q) or the amino acid alanine (A) or glycine (G) or serine (S) at position 99 in the count according to SEQ ID NO. 1. 1. A liquid washing or cleaning agent , comprising(a1) a protease containing an amino acid sequence that is at least 80% identical to the amino acid sequence listed in SEQ ID NO: 1 and that has an amino acid glutamic acid (E) or aspartic acid (D) at location 99 in a count according to SEQ ID NO: 1, or(a2) a protease containing an amino acid sequence that is at least 80% identical to the amino acid sequence listed in SEQ ID NO: 1 and that has an amino acid asparagine (N) or glutamine (Q) at location 99 in a count according to SEQ ID NO: 1, or(a3) a protease containing an amino acid sequence that is at least 80% identical to the amino acid sequence listed in SEQ ID NO: 1 and that has an amino acid alanine (A) or glycine (G) or serine (S) at location 99 in a count according to SEQ ID NO: 1, and(b) an amylase.2. The washing or cleaning agent according to claim 1 , wherein the protease further comprises at least one of the following amino acids in the count according to SEQ ID NO: 1:(a) threonine at location 3 (3T),(b) isoleucine at location 4 (4I),(c) alanine, threonine, or arginine at location 61 (61A, 61T or 61R),(d) aspartic acid or glutamic acid at location 154 (154D or 154E),(e) proline at location 188 (188P),(f) methionine at location 193 (193M),(g) isoleucine at location 199 (199I),(h) aspartic acid, glutamic acid, or glycine at location 211 (211D, 211E or 211G), and(i) combinations of the amino acids ...

Subtilase Variants

The present invention relates to novel subtilase variants exhibiting alterations relative to the parent subtilase in one or more properties including: Wash performance, thermal stability, storage stability or catalytic activity. The variants of the invention are suitable for use in e.g. cleaning or detergent compositions, such as laundry detergent compositions and dishwash compositions, including automatic dishwash compositions. 1. A subtilase variant comprising at least one or more of the following alterations:X11{A,R,N,D,C,Q,E,G,H,I,L,K,M,F,S,T,W,Y,V}, deletion, insertion;X30{A,R,N,D,C,Q,E,G,H,I,L,K,M,F,P,S,T,W,Y,V}, deletion, insertion;X31{R,N,D,Q,E,H,K,M,P,W,Y}, deletion, insertion;X32{A,R,D,C,E,G,H,I,L,K,M,F,P,T,W,Y,V}, insertion;X34{A,R,N,D,C,Q,E,G,H,I,L,K,M,F,S,T,W,Y,V}, deletion;X65{A,R,C,G,H,I,L,K,M,F,T,W,Y,V}, deletion, insertion;X66{A,R,C,H,I,L,K,M,F,T,W,Y,V}, deletion, insertion;X67{A,R,N,Q,G,H,I,K,M,F,P,S,T,W,Y,V};X68{R,N,D,Q,E,G,H,I,L,K,F,P,S,T,W,Y,V}, deletion, insertion;X69{A,R,N,D,Q,E,G,H,I,L,K,M,F,P,S,T,W,Y,V}, deletion, insertion;X70G;X71T;X77N;X83G, insertion;X84V;X85{A,R,N,D,Q,E,G,H,I,L,M,F,S,T,W,Y,V};X90{A,R,N,D,C,Q,E,G,H,I,L,K,M,F,P,S,T,W,Y,V}, deletion, insertion;X95{R,K,F,W,Y,V}, deletion;X107IX110G, insertion;X121V, insertion;X122 insertion;X123N;X125S;X150{A,R,N,D,Q,E,G,H,I,L,K,M,F,P,S,T,W,Y,V}, deletion, insertion;X152{A,R,N,D,Q,E,H,K,F,P,W,Y,V};X153{R,N,D,Q,E,G,H,I,L,K,M,F,T,W,Y,V};X154{A,R,G,H,I,L,M,F,W,Y,V};X164{A,R,H,T,W};X165{R,L,F,W,Y};X166{W,Y}, insertion;X175{R,N,D,Q,E,G,H,K,M,F,P,T,W,Y,V};X177{R,N,D,Q,E,G,H,I,L,K,M,F,P,S,T,W,Y,V}, deletion, insertion;X178{A,R,N,D,C,Q,E,G,H,I,L,K,M,F,P,S,T,W,Y,V}, deletion, insertion;X180{A,R,N,D,C,Q,E,G,H,I,L,K,M,F,P,S,T,W,Y,V}, deletion, insertion;X199{R,L,K,F,W,Y,V}, deletion, insertion;X200{A,R,I,L,K,M,F,W,Y,V}, deletion, insertion;X201{A,R,H,I,L,K,M,F,P,T,W,Y,V}, deletion, insertion;X202{A,R,C,G,H,I,L,K,M,F,T,W,Y,V};X207{A,R,N,C,Q,G,H,I,L,K,M,F,P,S,T,W,Y,V};X220T, insertion;X223A, insertion; ...

LIQUID CLEANING COMPOSITIONS

Disclosed are cleaning compositions and methods for cleaning fabrics to which stains are adhered. The cleaning composition contains a surfactant system comprising one or more anionic surfactants, a cleaning enzyme, and an organic acidulant having a calculated stability constant for Ca ions of less than about 1.5 at a pH of about 4. The cleaning composition has a neat pH of from about 2 to about 6. 1. A liquid cleaning composition comprising:a) from about 10% to about 60%, by weight of the liquid cleaning composition, of a surfactant system comprising from about 20% to about 97%, by weight of the surfactant system, of one or more anionic surfactants;b) from about 0.0001% to about 5%, by weight of the liquid cleaning composition, of a cleaning enzyme; and{'sup': '2+', 'c) from about 2% to about 20%, by weight of the liquid cleaning composition, of an organic acidulant having a calculated stability constant for Ca ion of less than about 1.5 at a pH of about 4;'}wherein the cleaning composition has a neat pH of from about 2 to about 6.2. The cleaning compositions of claim 1 , wherein the organic acidulant donates only one proton per molecule.3. The cleaning compositions of claim 1 , wherein the organic acidulant is an alpha-hydroxy acid.4. The cleaning composition of claim 1 , wherein the organic acidulant comprises lactic acid claim 1 , acetic acid claim 1 , or mixtures thereof.5. The cleaning composition of claim 1 , wherein the organic acidulant comprises lactic acid.6. The cleaning composition of claim 1 , wherein the cleaning composition comprises from about 4% to about 15% claim 1 , by weight of the liquid cleaning composition claim 1 , of the organic acidulant.7. The cleaning composition of claim 1 , wherein the cleaning composition comprises from about 5% to about 10% claim 1 , by weight of the liquid cleaning composition claim 1 , of the organic acidulant.8. The cleaning composition of claim 1 , wherein the organic acidulant has a calculated stability constant ...

Alpha-Amylase Mutants with Altered Properties

The present invention relates to variants (mutants) of parent Termamyl-like alpha-amylases, which variant has alpha-amylase activity and exhibits altered stability, in particular at high temperatures and/or at low pH relative, and/or low Ca to the parent alpha-amylase. 1. A variant of an alpha-amylase having at least 60% homology to SEQ ID NO. 8 , comprising an alteration at one or more positions selected from the group consisting of:49, 60, 104, 132, 161, 170, 176, 179, 180, 181, 183, 200, 203, 204, 207, 212, 237, 239, 250, 280, 298, 318, 374, 385, 393, 402, 406, 427, 430, 440, 444, 447, and 482, [ (i) an insertion of an amino acid downstream of the amino acid which occupies the position,', '(ii) a deletion of the amino acid which occupies the position, or', '(iii) a substitution of the amino acid which occupies the position with a different amino acid,, '(a) the alteration(s) are independently'}, '(b) the variant has alpha-amylase activity, and', '(c) each position corresponds to a position of the amino acid sequence of the alpha-amylase having the amino acid sequence shown in SEQ ID NO: 8., 'wherein'}2. The variant of claim 1 , which variant has one or more of the following mutations: T49I; D60N; N104D; E132A claim 1 ,V claim 1 ,P; D161N; K170Q; K176R; G179N; K180T; A181N; D183N; D200N; X203Y; D2045; D207V claim 1 ,E claim 1 ,L claim 1 ,G; X2121; K237P; S239W; E250G claim 1 ,F; N280S; X298Q; L318M; Q374R; E385V; Q393R; Y402F; H406L claim 1 ,W; L427I D430N; V440A; N444R claim 1 ,K; E447Q claim 1 ,K; Q482K using SEQ ID NO: 8 for the numbering.3. The variant of claim 1 , wherein the variant has the following mutations: G48A+T49I;G48A+T49I+G107A;G48A+T49I+G107A+I201F;G48A+T49I+I201F;T49I+G107A;T49I+G107A+I201F;T49I+E132V+V440A;T49I+K176R+D207V+Y402F;T49I+I201F;D60N+D207V+L318M;N104D+D161N+G179N+K180T+A181N+D183N+D200N+D204S+K237P+S239W;N104D+D161N+G179N+K180T+A181N+D183N+D200N+D204S+K237P+S239W+H406W+D430N+N444K+E447Q+Q482K; E132A+D207V;N104D+D161N+G179N+K180T+A181N+ ...

Detergent Compositions Comprising Metalloproteases

The present invention relates to the use of Thermolysin-Like Metalloproteases in cleaning processes, such as laundry and dish wash, and in particular to the use in low temperature wash and in removal of egg stains. The invention also relates to detergent compositions and cleaning compositions comprising Thermolysin-Like Metalloproteases.

Proteases With Modified Pro Regions

The present invention provides methods and compositions for the production of mature proteases in bacterial host cells. The compositions include modified polynucleotides that encode modified proteases, which have at least one mutation in the pro region; the modified serine proteases encoded by the modified polynucleotides; expression cassettes, DNA constructs, and vectors comprising the modified polynucleotides that encode the modified proteases; and the bacterial host cells transformed with the vectors of the invention. The methods include methods for enhancing the production of mature proteases in bacterial host cells e.g. sp. host cells. The produced proteases find use in the industrial production of enzymes, suitable for use in various industries, including but not limited to the cleaning, animal feed and textile processing industry. 1. An isolated modified polynucleotide encoding a modified protease , said isolated modified polynucleotide comprising a first polynucleotide encoding a signal peptide , said first polynucleotide being operably linked to a second polynucleotide encoding the pro region set forth in SEQ ID NO:7 , wherein said pro region comprises a substitution selected from the group consisting of: E6A , E6C , E6F , E6L , E6P , E6T , E6W , E6Y , E30A , E30I , E30L , E30P , E30T , E30V , E30Y , A32C , A32E , A32G , A32K , A32Q , A32S , and A32T , said second polynucleotide being operably linked to a third polynucleotide encoding the mature region of a protease that is at least about 60% identical to the mature protease of SEQ ID NO: 9.2Bacillus clausiiBacillus lentus.. The isolated modified polynucleotide of claim 1 , wherein said mature protease is a wild-type or variant alkaline serine protease derived from or3. (canceled)4. The isolated polynucleotide of claim 1 , wherein said signal peptide has an amino acid sequence chosen from SEQ ID NOS:3 and 5.5. (canceled)6. (canceled)7Bacillus. The isolated polynucleotide of claim 1 , wherein said ...

ENZYME GRANULE BLENDS CONSISTING ESSENTIALLY OF SODIUM SULFATE

The present teachings provide ways of improving the distribution of high payload enzyme granules by reducing their size, and by mixing them with size-matched dummy particles containing sodium sulfate. The present teachings also provide methods of using the mixtures. 1. A mixture consisting essentially of;a small enzyme granule, wherein at least 80% of the small enzyme granule comprises a diameter of about 300-400 microns; and,a size-matched sodium sulfate dummy particle, wherein at least 80% of the size-matched sodium sulfate dummy particle comprises a diameter of about 300-400 microns,wherein the median size of the small enzyme granule and the median size of the sodium sulfate dummy particle are size-matched such that they vary by less than 20 microns.2. The mixture of wherein the sodium sulfate is anhydrous.3. The mixture of wherein the small enzyme granule comprises a sodium sulfate core claim 1 , and at least one layer surrounding the core claim 1 , wherein the at least one layer surrounding the core comprises enzyme.4. The mixture of wherein the enzyme is a protease.5. A method of washing dishes comprising contacting the dishes with the mixture of .6. A method of washing clothes comprising contacting the clothes with the mixture of .7. A method of feeding animals comprising providing an animal feed to an animal in need of such feed claim 1 , wherein the feed comprises the mixture according to . The present application claims priority to International Patent Application No.: PCT/CN2011/071678, filed on Mar. 10, 2011, and which is incorporated by reference it's entirety.The present teachings relate to the field of enzyme granules, and improved compositions with reduced cost and improved functionality. Methods of use are also provided.There is a need for lower cost enzyme granules for use in a variety of applications, including detergents, textiles, baking and steam-pelleted animal feed. These applications generally benefit from enzymes that are protected from ...

Subtilase Vairants

The present invention relates to enzymes produced by mutating the genes for a number of subtilases and expressing the mutated genes in suitable hosts are presented. The enzymes exhibit improved stability and/or improved wash performance in any detergent in comparison to their wild type parent enzymes. The enzymes are well-suited for use in any detergent and for some in especially liquid or solid shaped detergent compositions. 171-. (canceled)72. A modified subtilisin BPN′ comprising a substitution of Lys at position 136 with Ala , Asn , Cys , Gln , Gly , His , Ser , Thr , or Tyr , wherein each position corresponds to a position of the amino acid sequence of subtilisin BPN′.73. The modified subtilisin BPN′ of claim 72 , further comprising at least one further mutation at one or more of positions: 27 claim 72 , 36 claim 72 , 57 claim 72 , 76 claim 72 , 97 claim 72 , 101 claim 72 , 104 claim 72 , 120 claim 72 , 123 claim 72 , 194 claim 72 , 206 claim 72 , 218 claim 72 , 222 claim 72 , 224 claim 72 , 235 and 274.74. The modified subtilisin BPN′ of claim 73 , wherein at least one further mutation is selected from the group consisting of K27R claim 73 , *36D claim 73 , S57P claim 73 , N76D claim 73 , G97N claim 73 , S101G claim 73 , V104A claim 73 , V104N claim 73 , V104Y claim 73 , H120D claim 73 , N123S claim 73 , A194P claim 73 , Q206E claim 73 , N218S claim 73 , M222A claim 73 , M222S claim 73 , T224S claim 73 , K235L claim 73 , and T274A.75. A detergent composition comprising a modified subtilisin BPN′ of and a surfactant.76. An isolated nucleic acid encoding a modified subtilisin BPN′ of .77. A vector comprising a nucleic acid of .78. A microbial host cell comprising a vector of .79. A method for producing a modified subtilisin BPN′ claim 77 , which comprises{'claim-ref': {'@idref': 'CLM-00078', 'claim 78'}, '(a) culturing a microbial host cell of under conditions conducive to the expression and secretion of the modified subtilisin BPN′, and'}(b) recovering the ...

METHODS OF TREATING A SURFACE AND COMPOSITIONS FOR USE THEREIN

This invention relates to compositions comprising certain fungal serine proteases and methods of treating a surface, preferably a textile using such compositions including the use of such compositions to clean a surface. 1. A method for cleaning a surface comprising (i) a first step of contacting said surface with a concentrated cleaning composition comprising a fungal serine protease; and (ii) a second step wherein the concentrated cleaning composition is diluted to form an aqueous wash liquor.2. A method according to wherein the concentrated cleaning composition comprises cleaning active components.3. A method according to wherein the surface is a textile surface.4. A method according to wherein the surface is contacted with the concentrated cleaning composition for at least one minute prior to the second claim 1 , dilution step.5. A method according to wherein the fungal serine protease is selected from the group consisting of:i) fungal serine protease having at least 56%, 70%, 75%, 80%, 85%, 90%, 95%, 99%, or even complete identity to SEQ ID NO: 1ii) fungal serine protease having at least 66%, 70%, 75%, 80%, 85%, 90%, 95%, 99%, or even complete identity to SEQ ID NO: 2iii) fungal serine protease having at least 66%, 70%, 75%, 80%, 85%, 90%, 95%, 99%, or even complete identity to SEQ ID NO: 3;iv) fungal serine protease having at least 86%, 90%, 95%, 99%, or even complete identity to SEQ ID NO: 4;v) fungal serine protease having at least 86%, 90%, 95%, 99%, or even complete identity to SEQ ID NO: 5;vi) fungal serine protease having at least 81%, 85%, 90%, 95%, 99%, or even complete identity to SEQ ID NO: 6; and mixtures thereof.6. A method according to wherein the composition comprises additional enzyme comprises a mannanase.7. A method according to wherein the composition comprises an additional enzyme comprising an amylase.8. A method according to wherein the concentrated cleaning and/or treatment composition comprises less than 70 wt % free water.9. A method ...

THERMOLYSIN VARIANTS AND DETERGENT COMPOSITIONS THEREWITH

The present invention provides methods and compositions comprising at least one thermolysin-like neutral protease enzyme with improved storage stability and/or catalytic activity. In some embodiments, the thermolysin finds use in cleaning and other applications comprising detergent. In some particularly preferred embodiments, the present invention provides methods and compositions comprising thermolysin formulated and/or engineered to resist detergent-induced inactivation. 14-. (canceled)5. An isolated thermolysin variant wherein said thermolysin has at least 95% amino acid identity with the amino acid sequence set forth in SEQ ID NO: 3.6. The thermolysin variant of claim 5 , wherein said thermolysin variant comprises the amino acid sequence set forth in SEQ ID NO: 3.7. (canceled)8Geobacillus. The isolated thermolysin variant of claim 5 , wherein said thermolysin variant is a thermolysin variant having an amino acid sequence comprising one or more substitutions at positions chosen from positions equivalent to positions 6 claim 5 , 7 claim 5 , 49 claim 5 , 56 claim 5 , 58 claim 5 , 61 claim 5 , 63 claim 5 , 65 claim 5 , 75 claim 5 , 128 claim 5 , 151 claim 5 , 156 claim 5 , 196 claim 5 , 273 claim 5 , 278 claim 5 , and 280 of the amino acid sequence set forth as SEQ ID NO: 3.9. (canceled)10Geobacillus. The isolated thermolysin variant of claim 5 , wherein said thermolysin variant is a thermolysin variant having an amino acid sequence comprising one or more substitutions at positions chosen from positions equivalent to positions 4 claim 5 , 6 claim 5 , 7 claim 5 , 36 claim 5 , 49 claim 5 , 53 claim 5 , 56 claim 5 , 58 claim 5 , 61 claim 5 , 63 claim 5 , 65 claim 5 , 75 claim 5 , 85 claim 5 , 108 claim 5 , 128 claim 5 , 129 claim 5 , 151 claim 5 , 156 claim 5 , 194 claim 5 , 195 claim 5 , 196 claim 5 , 261 claim 5 , 265 claim 5 , 273 claim 5 , 278 claim 5 , 280 and 297 of the amino acid sequence set forth as SEQ ID NO: 3.11. (canceled)12. The isolated thermolysin ...

SERINE PROTEASES

The present disclosure relates to serine proteases and variants thereof. Compositions containing the serine proteases are suitable for use in cleaning fabrics and hard surfaces, as well as in a variety of industrial applications. 1. A composition comprising a surfactant and a recombinant polypeptide or an active fragment thereof comprising an amino acid sequence having at least 93% amino acid sequence identity to an amino acid sequence selected from the group consisting of SEQ ID NOs:3 , 6 , 9 , and 12.2. The composition of claim 1 , with the proviso that the polypeptide or active fragment thereof does not comprise WP_034632645 or WP_047986748.3. The composition of claim 1 , wherein the polypeptide has protease activity.4. The composition of claim 3 , wherein the protease activity is subtilisin protease activity.5. The composition of claim 1 , wherein the polypeptide has protease activity in the presence of a surfactant.6. The composition of claim 1 , wherein the polypeptide has cleaning activity in a detergent composition.7. The composition of of claim 6 , wherein the detergent composition is an automatic dishwashing detergent and claim 6 , optionally claim 6 , wherein the cleaning activity comprises hydrolysis of an egg yolk substrate.8. The composition of claim 6 , wherein the detergent composition is a laundry detergent and claim 6 , optionally claim 6 , wherein the cleaning activity comprises hydrolysis of a substrate selected from the group consisting of blood claim 6 , milk claim 6 , ink and combinations thereof.9. The composition of claim 8 , wherein the laundry detergent is a liquid laundry detergent or a powder laundry detergent.10. The composition of claim 1 , wherein the polypeptide has a thermostability Tvalue of at least 60° C.11. (canceled)12. The composition of claim 1 , wherein the surfactant is selected from the group consisting of an anionic surfactant claim 1 , a cationic surfactant claim 1 , a zwitterionic surfactant claim 1 , an ampholytic ...

VARIANT MALTOHEXAOSE-FORMING ALPHA-AMYLASE VARIANTS

Disclosed are compositions and methods relating to variant maltohexaose-forming alpha-amylases. The variant alpha-amylases are useful, for example, for starch liquefaction and saccharification, for cleaning starchy stains in laundry, dishwashing, and other applications, for textile processing (e.g., desizing), in animal feed for improving digestibility, and for baking and brewing. 1. A variant α-amylase polypeptide derived from a parental α-amylase polypeptide , comprising at least two combinable mutations at productive amino acid positions; wherein:(i) each combinable mutation is the substitution of an amino acid residue present in the parental α-amylase with a different amino acid residue, which improves at least one desirable property of the variant α-amylase compared to the parental α-amylase, while not significantly decreasing either expression, activity, or stability of the variant α-amylase, compared to the parental α-amylase,(ii) a productive position is an amino acid position that can be substituted with a plurality of different amino acid residues, each of which substitutions result in a variant α-amylase that meets the requirements of (i), and(iii) the combinable mutation corresponds to a mutation listed in Lists A, B, C, or D, or in Table C or D, which use SEQ ID NO: 3 for numbering wherein,the combinable mutations produce a variant amylase wherein the minimum performance indices (PI) relative to the parental amylase for (i) protein expression, (ii) activity, and (iii) detergent stability or thermostability are greater than or equal to 0.8, and the PI for any one of (i), (ii), or (iii) that is greater than or equal to 1.2, orthe combinable mutations produce a variant amylase wherein the minimum performance indices (PI) relative to the parental amylase for (i) protein expression, (ii) activity, and (iii) detergent stability or thermostability are greater than or equal to 0.5, and the PI for any one of (i), (ii), or (iii) that is greater than or equal to 1 ...

POLYPEPTIDES HAVING PROTEASE ACTIVITY AND POLYNUCLEOTIDES ENCODING SAME

Disclosed are isolated polypeptides having protease activity, and polynucleotides encoding the polypeptides. Nucleic acid constructs, vectors, and host cells comprising the polynucleotides as well as methods of producing and using the polypeptides are also disclosed. 1. An isolated polypeptide having protease activity , selected from the group consisting of:(a) a polypeptide having at least 90% to the mature polypeptide of SEQ ID NO: 2, or the mature polypeptide of SEQ ID NO: 4 and(b) a polypeptide encoded by a polynucleotide having at least 90% sequence identity to the mature polypeptide coding sequence of SEQ ID NO: 1, or to the mature polypeptide coding sequence of SEQ ID NO: 3, or a cDNA sequence thereof.2. The polypeptide of comprising or consisting of a) SEQ ID NO: 2 or the mature polypeptide of SEQ ID NO: 2 claim 1 , or b) SEQ ID NO: 4 or the mature polypeptide of SEQ ID NO: 4.3. The polypeptide of claim 2 , wherein the mature polypeptide is amino acids 1 to 288 of SEQ ID NO: 2 claim 2 , or amino acids 1 to 288 of SEQ ID NO: 4.4. The polypeptide of claim 1 , which is a variant of the mature polypeptide of SEQ ID NO: 2 or a variant of the mature polypeptide of SEQ ID NO: 4 comprising a substitution claim 1 , a deletion claim 1 , and/or an insertion at one or more positions.5. A composition comprising the polypeptide of .6. The composition of being a detergent composition.7. The composition of further comprising one of more additional enzymes selected among claim 5 , proteases claim 5 , amylases claim 5 , lipases claim 5 , cutinases claim 5 , cellulases claim 5 , endoglucanases claim 5 , xyloglucanases claim 5 , pectinases claim 5 , pectin lyases claim 5 , xanthanases claim 5 , peroxidaes claim 5 , haloperoxygenases claim 5 , catalases claim 5 , mannanases claim 5 , or any mixture thereof.8. The composition of comprising one or more components selected from the group consisting of surfactants claim 5 , builders claim 5 , chelators or chelating agents claim 5 , ...

Subtilisin Variants and Polynucleotides Encoding Same

The present invention relates to subtilisin variants and methods for obtaining subtilisin variants. The present invention also relates to polynucleotides encoding the variants; nucleic acid constructs, vectors, and host cells comprising the polynucleotides; and methods of using the variants. 1. A subtilisin variant having protease activity comprising the substitutions corresponding to Y217X and N218Z of SEQ ID NO 2 , wherein X and Z are selected from the group consisting of K , H , R , D , E , S and T , wherein when X is either K , H or R then Z is also selected from K , H or R , and wherein when X is either D , E , S or T then Z is also selected from D , E , S or T.2. The variant according to claim 1 , wherein X and Z are the same amino acid.3. The variant according to claim 2 , wherein X and Z are D or E.4. The variant according to claim 2 , wherein X and Z are K or R.5. The variant of claim 1 , which has at least 60%.6. The variant of claim 5 , wherein the length of alignment is at least 150 amino acid residues.7. The variant of claim 1 , wherein the variant consists of 150 to 350.8. The variant of claim 1 , wherein the number of alterations is 1-20.9. The variant of claim 1 , which comprises any of the substitutions selected from the group consisting of [Y217D+N218D] claim 1 , [Y217E+N218E] claim 1 , [Y217D+N218E] claim 1 , [Y217E+N218D] claim 1 , [Y217E+N218S] claim 1 , [Y217S+N218E] claim 1 , [Y217S+N218S] claim 1 , [Y217D+N218S] claim 1 , [Y217S+N218D] claim 1 , [Y217E+N218T] claim 1 , [Y217T+N218E] claim 1 , [Y217T+N218T] claim 1 , [Y217D+N218T] claim 1 , [Y217T+N218D] [Y217K+N218K] claim 1 , [Y217R+N218R] claim 1 , [Y217K+N218R] claim 1 , [Y217R+N218K] claim 1 , [Y217R+N218H] claim 1 , [Y217H+N218R] claim 1 , [Y217H+N218H] claim 1 , [Y217K+N218H] claim 1 , [Y217H+N218K].10. The variant of claim 1 , which has an improved wash performance on egg stains compared to the parent or compared to a protease with SEQ ID NO: 2.11. A composition comprising the variant ...

PROTEASES COMPRISING ONE OR MORE COMBINABLE MUTATIONS

The present invention provides engineered protease variants. In particular, the protease variants comprise combinable mutations at selected surface positions that affect the charge and/or hydrophobicity of the enzyme to enhance at least one desired property of the resulting variant enzyme in a chosen application. Compositions comprising the protease variants, and methods for using the same are also provided. 18-. (canceled)9BacillusB. amyloliquefaciens. An isolated nucleic acid encoding an isolated subtilisin protease variant of a parent subtilisin , wherein said subtilisin variant is a mature form having proteolytic activity and comprising a substitution at two or more positions selected from positions 24 , 45 , 101 , 109 , 118 , 213 and 217 , wherein said positions are numbered by correspondence with the amino acid sequence of subtilisin BPN′ set forth as SEQ ID NO:1 , and wherein said parent has the sequence of SEQ ID NO:4 or SEQ ID NO:7.10. An expression vector comprising the nucleic acid of .11. A host cell comprising the expression vector set forth .1219-. (canceled)20. The nucleic acid of claim 9 , wherein said isolated subtilisin variant further comprises a relative protein expression level performance index (TCA PI) and/or a stain removal activity performance index (BMI PI) that is greater than or equal to 0.5.21Bacillus. The nucleic acid of claim 20 , wherein said parent subtilisin of said isolated subtilisin variant is GG36 and wherein said substitution at two or more positions is selected from: S24Q claim 20 , S24E claim 20 , S24L claim 20 , S24R claim 20 , R45Q claim 20 , R45E claim 20 , R45L claim 20 , S101Q claim 20 , S101E claim 20 , S101L claim 20 , S101R claim 20 , Q109E claim 20 , Q109L claim 20 , Q109 R claim 20 , G118Q claim 20 , G118E claim 20 , G118L claim 20 , G118R claim 20 , T213Q claim 20 , T213L claim 20 , T213R claim 20 , T213E claim 20 , L217Q claim 20 , and L217E claim 20 , wherein the positions correspond to the positions of BPN′ ...

Subtilases

The present invention relates to methods for producing variants of a parent TY145 subtilase and of a parent BPN′ subtilase and to TY145 and BPN′ variants having altered properties as compared to the parent TY145/BPN′ subtilase.

SERINE PROTEASES OF BACILLUS SPECIES

The present disclosure relates to serine proteases cloned from spp., and variants thereof. Compositions containing the serine proteases are suitable for use in cleaning fabrics and hard surfaces, as well as in a variety of industrial applications. 2. The composition according to claim 1 , wherein the subtilisin or recombinant polypeptide or active fragment thereof further comprises an amino acid sequence having at least 70% amino acid sequence identity to an amino acid sequence selected from the group consisting of SEQ ID NOs:3 claim 1 , 6 and 9.3. The composition according to claim 1 , with the proviso that the subtilisin and/or recombinant polypeptide or active fragment thereof does not comprise BAD02409 or JP2003325186-0001.4. The composition of claim 1 , wherein the subtilisin and/or recombinant polypeptide or active fragment has protease activity.5. A composition comprising a surfactant and a recombinant polypeptide or an active fragment thereof comprising an amino acid sequence having at least 80% amino acid sequence identity to an amino acid sequence selected from the group consisting of SEQ ID NOs:3 claim 1 , 6 and 9.68-. (canceled)9. The composition of claim 5 , with the proviso that the recombinant polypeptide or active fragment thereof does not comprise BAD02409 or JP2003325186-0001.10. The composition of claim 5 , wherein the polypeptide has protease activity.11. The composition of claim 10 , wherein the protease activity comprises casein hydrolysis activity or dimethlycasein hydrolysis activity.12. The composition of claim 5 , wherein the polypeptide retains at least 50% of its maximal protease activity at a pH range of 6 to 12 and/or a temperature range of 55° C. to 80° C.13. The composition of claim 5 , wherein the polypeptide retains at least 60% activity after 20 minutes at 50° C. under stressed conditions.14. The composition of claim 13 , wherein the stressed condition is in an LAS/EDTA or OMO HDL assay.15. The composition of claim 5 , wherein the ...

SUBTILASE VARIANTS AND COMPOSITIONS COMPRISING SAME

The invention relates to subtilase variants and detergent compositions comprising the variants, as well as methods of producing the variants and methods for stabilizing a subtilase variant. 1. A subtilase variant , comprising mutations at three or more positions selected from the group consisting of 9 , 63 , 76 , 88 , 104 , 107 , 128 , 131 , 159 , 204 , 206 , 209 , 212 , 215 , 216 , 261 and 262 , wherein positions are numbered according to SEQ ID NO: 1 , and wherein the variant has protease activity and a sequence identity to SEQ ID NO: 1 of at least 80% and less than 100%.2. The subtilase variant of claim 1 , wherein the variant comprises mutations at three or more positions selected from the group consisting of:(i) 209 in combination with two or more mutations at positions selected from 63, 215 and 217;(ii) 104 and 128 in combination with at least one mutation at a position selected from 9, 63, 76, 107, 131, 159, 204, 206, 212, 215, 216 and 217;(iii) 9 in combination with at least two mutations at positions selected from 76, 204 and 212;(iv) 76 in combination with at least two mutations at positions selected from 9, 88, 159, 204, 206, 212, 216, 261 and 262;(v) 206 in combination with at least two mutations at positions selected from 9, 76, 159, 204, 209, 212, 216, 217, 261 and 262; and(vi) 204, 212 and 216, in combination with at least one mutation at a position selected from 9, 159 and 206.3. The subtilase variant of claim 1 , wherein:the mutation in position 9 is S9E or S9D,the mutation in position 63 is S63G or S63A,the mutation in position 76 is N76D or N76E,the mutation in position 88 is A88V, A88I, A88L or A88M,the mutation in position 104 is Y104V, Y104I, Y104L or Y104M,the mutation in position 107 is I107L, I107V, I107M,the mutation in position 128 is G128S, G128A or G128T,the mutation in position 131 is G131* or G131P,the mutation in position 159 is S159E or S159D,the mutation in position 204 is S204D or S204E,the mutation in position 206 is Q206L, Q206I, ...

USE AND PRODUCTION OF STORAGE-STABLE NEUTRAL METALLOPROTEASE

The present invention provides methods and compositions comprising at least one neutral metalloprotease enzyme that has improved storage stability. In some embodiments, the neutral metalloprotease finds use in cleaning and other applications. In some particularly preferred embodiments, the present invention provides methods and compositions comprising neutral metalloprotease(s) obtained from sp. In some more particularly preferred embodiments, the neutral metalloprotease is obtained from . In still further preferred embodiments, the neutral metalloprotease is a variant of the neutral metalloprotease. In yet additional embodiments, the neutral metalloprotease is a homolog of the the neutral metalloprotease. The present invention finds particular use in applications including, but not limited to cleaning, bleaching and disinfecting. 114-. (canceled)15. An isolated neutral metalloprotease variant having an amino acid sequence comprising at least one substitution of an amino acid made at a position equivalent to a position in a neutral metalloprotease comprising the amino acid sequence set forth in SEQ ID NO: 18 , wherein said protease comprises at least one mutation selected from T004C , T004E , T004H , T004I , T004K , T004L , T004M , T004N , T004P , T004R , T004S , T004V , T004W , T004Y , G012D , G012E , G012I , G012K , G012L , G012M , G012Q , G012R , G012T , G012V , G012W , K013A , K013C , K013D , K013E , K013F , K013G , K013H , K013I , K013L , K013M , K013N , K013Q , K013S , K013T , K013V , K013Y , T014F , T014G , T014H , T014I , T014K , T014L , T014M , T014P , T014Q , T014R , T014S , T014V , T014W , T014Y , S023A , S023D , S023F , S023G , S023I , S023K , S023L , S023M , S023N , S023P , S023Q , S023R , S023S , S023T , S023V , S023W , S023Y , G024A , G024D , G024F , G024G , G024H , G024I , G024K , G024L , G024M , G024N , G024P , G024R , G024S , G024T , G024V , G024W , G024Y , K033H , Q045C , Q045D , Q045E , Q045F , Q045H , Q045I , Q045K , Q045L , Q045M , Q045N , ...

STORAGE-STABLE LIQUID DISHWASHING DETERGENT CONTAINING PROTEASE AND AMYLASE

In a liquid dishwashing detergent comprising a protease and amylase, storage stability is to be improved. This is achieved through the use of a protease comprising an amino acid sequence having at least 70% identity over its total length with the amino acid sequence specified in SEQ ID NO. 1 and having, in the listing according to SEQ ID NO. 1, the L211D amino acid substitution in combination with at least two further amino acid substitutions selected from the group consisting of S3T, V4I, V193M and V199I. 1. A liquid dishwashing detergent comprising(a) a protease comprising an amino acid sequence having at least 70% identity over its total length with the amino acid sequence specified in SEQ ID NO. 1 and having, in the listing according to SEQ ID NO. 1, the L211D amino acid substitution in combination with at least two further amino acid substitutions selected from the group consisting of S3T, V4I, V193M and V199I, and(b) an amylase.2. The dishwashing detergent according to claim 1 , wherein the protease comprises an amino acid sequence having at least 71% claim 1 , 72% claim 1 , 73% claim 1 , 74% claim 1 , 75% claim 1 , 76% claim 1 , 77% claim 1 , 78% claim 1 , 79% claim 1 , 80% claim 1 , 81% claim 1 , 82% claim 1 , 83% claim 1 , 84% claim 1 , 85% claim 1 , 86% claim 1 , 87% claim 1 , 88% claim 1 , 89% claim 1 , 90% claim 1 , 90.5% claim 1 , 91% claim 1 , 91.5% claim 1 , 92% claim 1 , 92.5% claim 1 , 93% claim 1 , 93.5% claim 1 , 94% claim 1 , 94.5% claim 1 , 95% claim 1 , 95.5% claim 1 , 96% claim 1 , 96.5% claim 1 , 97% claim 1 , 97.5% claim 1 , 98% or 98.5% identity over its total length with the amino acid sequence specified in SEQ ID NO. 1 and having claim 1 , in the listing according to SEQ ID NO. 1 claim 1 , the L211D amino acid substitution in combination with the S3T claim 1 , V4I claim 1 , V193M and V199I amino acid substitutions.3. The dishwashing detergent according to claim 1 , whereinthe protease at position 99 has the amino acid arginine (R),the ...

POLYPEPTIDES HAVING ALPHA AMYLASE ACTIVITY

The present invention relates to polypeptides having alpha-amylase activity and polynucleotides encoding the polypeptides. The invention also relates to nucleic acid constructs, vectors, and host cells comprising the polynucleotides as well as methods of producing and using the polypeptides. 1. A polypeptide having alpha-amylase activity comprising an A and B domain and a C domain , wherein the amino acid sequence of said A and B domain is at least 75% identical to the amino acid sequences of SEQ ID NO: 2 , 15 , 20 , 26 , 29 , 32 , 39 , or 23; and the amino acid sequence of said C domain is at least 75% identical to the amino acid sequence of SEQ ID NO: 6.2. The polypeptide according to claim 1 , wherein said A and B domain has at least 80% claim 1 , at least 85% claim 1 , at least 90% claim 1 , at least 91% claim 1 , at least 92% claim 1 , at least 93% claim 1 , at least 94% claim 1 , at least 95% claim 1 , at least 96% claim 1 , at least 97% claim 1 , at least 98% claim 1 , at least 99% or 100% sequence identity to the A and B domain having the amino acid sequence selected from the group consisting of SEQ ID NO: 2 claim 1 , SEQ ID NO: 15 claim 1 , SEQ ID NO. 20 claim 1 , SEQ ID NO. 26 claim 1 , SEQ ID NO. 29 claim 1 , SEQ ID NO. 32 claim 1 , SEQ ID NO. 39 claim 1 , and SEQ ID NO. 23.3. (canceled)4. (canceled)5. (canceled)6. (canceled)7. (canceled)8. (canceled)9. (canceled)10. The polypeptide according to claim 1 , wherein said C domain has at least 80% claim 1 , at least 85% claim 1 , at least 90% claim 1 , at least 91% claim 1 , at least 92% claim 1 , at least 93% claim 1 , at least 94% claim 1 , at least 95% claim 1 , at least 96% claim 1 , at least 97% claim 1 , at least 98% claim 1 , at least 99% or 100% sequence identity to the C domain having the amino acid sequence of SEQ ID NO: 6 claim 1 , SEQ ID NO: 10 claim 1 , SEQ ID NO: 11 claim 1 , or SEQ ID NO. 12.11. (canceled)12. (canceled)13. (canceled)14. The polypeptide according to comprising a deletion of one ...

DETERGENT COMPOSITION COMPRISING PROTEASE AND AMYLASE VARIANTS

The present invention relates to detergent compositions comprising protease variants and alpha-amylases or variants thereof. Furthermore, the present invention relates to methods of using the detergent compositions. 1. A detergent composition comprising (i) at least one protease variant comprisinga substitutionat one or more positions corresponding to positions 171, 173, 175, 179, or 180 of SEQ ID NO:1, wherein said protease variant has a sequence identity of at least 75% but less than 100% to SEQ ID NO: 1, and wherein the protease variant has protease activity, and (ii) at least one alpha-amylase having the amino acid sequence of SEQ ID NO: 2, 3, 4, 5, 6, 7, 8, or 9, or a variant thereof having a sequence identity of at least 75% but less than 100% to SEQ ID NO: 4, 5, 6, 7, 8, or 9, and wherein said alpha-amylase variant has alpha-amylase activity.2. The detergent composition according to claim 1 , wherein said at least one protease variant comprises a substitution in at least one position corresponding to positions 173 claim 1 , 175 claim 1 , or 180 of SEQ ID NO: 1.3. The detergent composition according to claim 1 , wherein said at least one protease variant comprises a substitution in at least one position corresponding to positions 171 claim 1 , 173 claim 1 , 175 claim 1 , 179 claim 1 , or 180 claim 1 , and whereina. the amino acid in the position corresponding to position 171 of SEQ ID NO: 1 is selected from the group consisting of W, K, E,D and N; and/orb. the amino acid in the position corresponding to position 173 of SEQ ID NO: 1 is P; and/orc. the amino acid in the position corresponding to position 175 of SEQ ID NO: 1 is selected from the group consisting of A, V, and P; and/ord. the amino acid in the position corresponding to position 179 of SEQ ID NO: 1 is selected from the group consisting of C, V, Q, S, T, E, H, K, M, N, Y, and A; and/ore. the amino acid in the position corresponding to position 180 of SEQ ID NO: 1 is Y.4. The detergent composition ...

CHIMERIC ALPHA-AMYLASE VARIANTS

Chimeric alpha-amylases having the characteristics of high thermostability and good performance in starch degradation, especially high-temperature liquefaction processes, are provided. The alpha-amylases are chimeras of AmyL and AmyS enzymes, and are useful in starch degradation processes. Methods of making the chimeric enzymes, and methods of using the chimeric alpha-amylases for liquefaction, cleaning starch residue from a surface, and treating woven material to remove coatings. Kits for practicing the methods are provided. Polynucleotides encoding the chimeric amylases, vectors, and expression hosts also are provided. 1. A chimeric polypeptide having at least about 95% sequence identity to SEQ ID NO:11 , wherein said chimeric polypeptide has enhanced thermostability relative at least to a wild type AmyS amylase.29-. (canceled)10. The chimeric polypeptide of comprising a catalytic activity of an α-amylase that retains at least 50% of its activity after incubation at 95° C. for 30 minutes.11. The chimeric polypeptide of that retains at least about 60% of its catalytic activity after incubation at 95° C. for 60 minutes.12. The chimeric polypeptide of which retains at least about 80% of its catalytic activity after incubation at 95° C. for 60 minutes.1323-. (canceled)24. A composition comprising the chimeric polypeptide of .25. The composition of further comprising one or more additional polypeptides.26. The composition of claim 25 , wherein the one or more additional polypeptides is an enzyme.27. The composition of that includes one or more detergents or cleaning agents.28. The composition of that is formulated for use in food or food processes.29. A food-grade lyophilized composition comprising the composition of .30. A polynucleotide encoding the chimeric polypeptide of .31. (canceled)32. The polynucleotide of claim 30 , wherein the codon usage is optimized for expression of the chimeric polypeptide in a microorganism or a plant.33. A vector comprising the ...

Bacteria Cultures and Compositions Comprising Bacteria Cultures

The present invention relates to bacteria cultures and composition comprising one or more cultures of the invention. The invention also relates to methods of washing or cleaning laundry or fabrics and surfaces as well as degrading waste material using a bacteria culture of the invention. 1: A method for treating soils or stains on a surface comprising subjecting the soil or stain to one or more isolated bacterial strains selected from the group consisting of:the strain having the deposit accession number PTA-7541;the strain having the deposit accession number PTA-7542;the strain having the deposit accession number PTA-7543;the strain having the deposit accession number PTA-7544;the strain having the deposit accession number PTA-7545;the strain having the deposit accession number PTA-7546;the strain having the deposit accession number PTA-7547;the strain having the deposit accession number PTA-7548;the strain having the deposit accession number PTA-7549.the strain having the deposit accession number PTA-7550,the strain having the deposit accession number PTA-7789,the strain having the deposit accession number PTA-7790,the strain having the deposit accession number PTA-7791,the strain having the deposit accession number PTA-7792,the strain having the deposit accession number PTA-7793, ora mixture of two or more of the strains.2: The method of claim 1 , wherein the method further comprises subjecting the soil or stain to one or more enzymes.3: The method of claim 2 , wherein the one or more enzymes are selected from the group consisting of a protease claim 2 , an alpha-amylase claim 2 , a cellulase claim 2 , a lipase claim 2 , a peroxidase claim 2 , an oxidase claim 2 , a pectate lyase claim 2 , a mannase claim 2 , or mixtures thereof.4: The method of claim 1 , wherein the one or more bacterial strains is the strain having the deposit accession number PTA-7541.5: The method of claim 1 , wherein the one or more bacterial strains is the strain having the deposit ...

DISHWASHING LIQUID HAVING BLEACHING CATALYST AND PROTEASE

In a dishwashing liquid, the cleaning performance, in particular on bleachable stains such as, for example, tea stains, is to be improved. This succeeds using a dishwashing liquid which comprises a hydrogen peroxide source, a bleaching catalyst and a protease that, in native electrophoresis on a polyacrylamide gel, has a migration distance that is longer than the migration distance of the protease as per SEQ ID NO. 1. 1. A dishwashing agent comprising a hydrogen peroxide source , a bleach catalyst and a protease , wherein the protease in a native electrophoresis in a polyacrylamide gel has a migration distance that is longer than the migration distance of the protease according to SEQ ID NO: 1.2. The dishwashing agent according to claim 1 , wherein the bleach catalyst is selected from the group consisting of bleach boosting transition metal salts and transition metal complexes claim 1 , and the hydrogen peroxide source is selected from sodium percarbonate claim 1 , sodium perborate tetrahydrate or sodium perborate monohydrate or a combination hereof.3. The dishwashing agent according to wherein it comprises the protease in an amount of 1×10-10 wt % claim 1 , based on the total protein content of the protease claim 1 , the bleach catalyst in an amount of 0.0025-1 wt % claim 1 , and the hydrogen peroxide source in an amount of 2-30 wt %.4. The dishwashing agent according to claim 1 , further comprising a bleach activator in an amount of 0.1-10 wt %.5. The dishwashing agent according to one of to claim 1 , wherein:a. the calculated iso electric point of the protease is greater than 9.3;b. the calculated net charge of the protease is greater than 3.38; andc. the protease comprises an amino acid sequence that is at least 70% identical to the amino acid sequence selected from the group consisting of those listed in SEQ ID NO. 3, SEQ ID NO. 2, and SEQ ID NO. 1.6. The dishwashing agent according to claim 1 , wherein it is in solid form claim 1 , a free flowing powder claim ...

Enzyme and Inhibitor Containing Water-Soluble Films

The invention relates to enzyme and protease inhibitor containing water-soluble films, and their use in detergents.

Novel whitening agents for cellulosic substrates

This invention relates to novel whitening agents for cellulosic substrates. The whitening agents are comprised of at least two components: at least one chromophore component and at least one polymeric component. Suitable chromophore components generally fluoresce blue, red, violet, or purple color when exposed to ultraviolet light, or they may absorb light to reflect these same shades. The whitening agents are further characterized by having a dispersion component value of the Hansen Solubility Parameter of less than or equal to about 17 MPa 0.5 . This invention also relates to laundry care compositions including but not limited to liquid and/or powder laundry detergent formulations and rinse added fabric softening (RAFS) compositions that comprise such whitening agents.

Detergent Pouch with Enzymatic Water-Soluble Film

The invention relates to enzyme containing water-soluble films, and their use in detergents. 1. A method of making an enzyme containing water-soluble film , the method comprising use of a liquid enzyme formulation with an OD440 (10 mm path length) <0.15 per % AEP.2. A method of making an enzyme containing water-soluble film , the method comprising use of a liquid enzyme formulation with an odor threshold of less than 20 ppm AEP.3. A detergent pouch comprising a compartment formed by an enzyme containing water-soluble film , and an enzyme containing detergent , wherein the enzyme in the film is different from the enzyme in the detergent; preferably the enzyme in the film is protease.4. A detergent pouch comprising at least one compartment formed by at least two separate enzymes containing water-soluble films , and a detergent , wherein the enzymes in the two films are different. In an embodiment , one film contains a protease.5. A detergent pouch comprising a compartment formed by an enzyme containing water-soluble film , and a detergent containing a builder with a Ca logarithmic stability constant of above 4.5; preferably the detergent is a dishwash detergent.6. The detergent pouch of claim 5 , wherein the builder is a biodegradable chelating agent.7. A detergent pouch comprising a compartment formed by an enzyme containing water-soluble film claim 5 , and a liquid detergent containing a viscosity modifier which is a substrate for the enzyme.8. The detergent pouch of claim 7 , wherein the enzyme containing water-soluble film is a lipase containing water-soluble film claim 7 , and the viscosity modifier is hydrogenated castor oil.9. A detergent pouch comprising a compartment formed by a lipase containing water-soluble film claim 7 , a detergent claim 7 , and a fragrance ester.10. A detergent pouch comprising a compartment formed by an enzyme containing water-soluble film claim 7 , and a liquid detergent with an internal solvent system comprising at least one primary ...

MOLD AND FUNGAL (MYCOTOXIN) TOXIN REMEDIATION

A method of treating a building for mold contamination including the steps of assessing and locating mold growth areas, constructing a containment barrier around the mold growth areas, vacuuming, abrading and surface treating the mold growth areas, ceilings, walls and window treatments with mold cleaner, replacing air filters from air handlers, removing all registers and vent grills in the treated areas and washing the vent grills with mold cleaner, vacuuming all registers and accessible ductwork, treating the heating and ventilation system, associated ductwork and wall cavities with an atomized mold cleaner, vacuuming all flooring, horizontal surfaces, walls, furniture and mattresses, re-vacuuming all flooring, re-treating the heating and ventilation system and associated ductwork with an atomized mold cleaner and re-treating the work area including any exposed wall cavities with an atomized mold cleaner, deconstructing and discarding containment barrier and reinstalling all registers and vent grills. 1. A method of treating a building for mold contamination comprising the steps of:a. assessing and locating mold growth areas;b. constructing a containment barrier around one or more areas to be treated to isolate designated areas from the rest of the structure, if necessary;c. installing air scrubbers as needed;d. vacuuming, abrading and surface treating exposed framing with visible microbial growth;e. surface treating salvageable building materials with mold cleaner;f. removing air filters from air handlers and disposing the filters;g. removing all registers and vent grills in the treated areas;h. washing the vent grills with mold cleaner;i. vacuuming all registers and accessible ductwork;j. vacuuming the interior of the air handler;k. surface treating coils and sheet metal with mold cleaner;l. treating the heating and ventilation system and associated ductwork with a mold cleaner;m. treating the work area including any exposed wall cavities with a mold cleaner;n. ...

PERFORMANCE GEAR, TEXTILE TECHNOLOGY, AND CLEANING AND PROTECTING SYSTEMS AND METHODS

A cleaning system for laundry which includes a washing agent and a protective agent. The washing agent is configured to remove unwanted matter from the laundry. The protective agent is configured to create a bonded barrier comprising organosilane antimicrobial(s) on the laundry for protection against odors from bacteria, mold and mildew and/or the like. The washing agent and the protective agent are configured to be used in a two-step water-based treatment process in which the washing agent is provided in a given first step of the treatment process and the protective agent is provided in a given subsequent second step of the treatment process. 1. A cleaning system for natural and synthetic fabrics , high performance textiles , sports gear , towels and linens , the cleaning system comprising:a cleaning agent configured to remove unwanted matter from laundry, the cleaning agent comprising at least one chelator, a plurality of nonionic/cationic surfactants, at least one organosilane antimicrobial and a plurality of enzymes; anda protective agent configured to create a bonded barrier of protection against odors from at least one of bacteria, mold and mildew on the from laundry, the protective agent comprising at least one antistatic agent and at least one organosilane antimicrobial, and the bonded barrier comprising the at least one organosilane antimicrobial.2. The system of claim 1 , wherein the cleaning agent comprises claim 1 , by weight claim 1 , generally one percent chelator claim 1 , in a range of generally 20 to 72 percent nonionic/cationic surfactants claim 1 , generally 0.7 percent organosilane antimicrobial claim 1 , and generally 0.7 percent enzymes.3. The system of claim 1 , wherein the cleaning agent comprises claim 1 , by weight claim 1 , generally one percent chelator claim 1 , generally of 20 percent nonionic/cationic surfactants claim 1 , generally 0.7 percent organosilane antimicrobial claim 1 , and generally 0.7 percent enzymes.4. The system of ...

USE AND PRODUCTION OF STORAGE-STABLE NEUTRAL METALLOPROTEASE

The present invention provides methods and compositions comprising at least one neutral metalloprotease enzyme that has improved storage stability. In some embodiments, the neutral metalloprotease finds use in cleaning and other applications. In some particularly preferred embodiments, the present invention provides methods and compositions comprising neutral metalloprotease(s) obtained from sp. In some more particularly preferred embodiments, the neutral metalloprotease is obtained from In still further preferred embodiments, the neutral metalloprotease is a variant of the neutral metalloprotease. In yet additional embodiments, the neutral metalloprotease is a homolog of the the neutral metalloprotease. The present invention finds particular use in applications including, but not limited to cleaning, bleaching and disinfecting. 112-. (canceled)13. An isolated neutral metalloprotease variant having an amino acid sequence comprising multiple substitutions selected from V190F/D220P , V190I/D220P , V190I/D220E , and V190L/D220E , wherein said variant has at least 90% sequence identity to SEQ ID NO:18.14. The isolated neutral metalloprotease variant of claim 13 , wherein said variant further comprises at least one substitution at a position selected from at least one position equivalent to positions 1 claim 13 , 3 claim 13 , 4 claim 13 , 5 claim 13 , 6 claim 13 , 11 claim 13 , 12 claim 13 , 13 claim 13 , 14 claim 13 , 16 claim 13 , 21 claim 13 , 23 claim 13 , 24 claim 13 , 25 claim 13 , 31 claim 13 , 32 claim 13 , 33 claim 13 , 35 claim 13 , 36 claim 13 , 38 claim 13 , 44 claim 13 , 45 claim 13 , 46 claim 13 , 47 claim 13 , 48 claim 13 , 49 claim 13 , 50 claim 13 , 51 claim 13 , 54 claim 13 , 55 claim 13 , 58 claim 13 , 59 claim 13 , 60 claim 13 , 61 claim 13 , 62 claim 13 , 63 claim 13 , 65 claim 13 , 66 claim 13 , 69 claim 13 , 70 claim 13 , 76 claim 13 , 85 claim 13 , 86 claim 13 , 87 claim 13 , 88 claim 13 , 90 claim 13 , 91 claim 13 , 92 claim 13 , 96 claim 13 , 97 ...

Subtilase Variants

The present invention relates to novel subtilase variants exhibiting alterations relative to the parent subtilase in one or more properties including: Wash performance, thermal stability, storage stability or catalytic activity. The variants of the invention are suitable for use in e.g. cleaning or detergent compositions, such as laundry detergent compositions and dishwash compositions, including automatic dishwash compositions.

NOVEL METALLOPROTEASES

Aspects of the present compositions and methods relate to novel metalloproteases polynucleotides encoding the novel metalloprotease, compositions and methods for use thereof. 1. A polypeptide comprising an amino acid sequence having at least 60% sequence identity to an amino acid sequence selected from the group consisting of SEQ ID NO: 3 , 6 , 9 and 13.2. The polypeptide of claim 1 , wherein said polypeptide has at least 80% sequence identity to the amino acid sequence selected from the group consisting of SEQ ID NO: 3 claim 1 , 6 claim 1 , 9 and 13.3. The polypeptide of any of or claim 1 , wherein said polypeptide has at least 95% sequence identity to the amino acid sequence selected from the group consisting of SEQ ID NO: 3 claim 1 , 6 claim 1 , 9 and 13.4. The polypeptide of any of the above claims claim 1 , wherein said amino acid sequence is the amino acid sequence selected from the group consisting of SEQ ID NO: 3 claim 1 , 6 claim 1 , 9 and 13.5. The polypeptide of any of the above claims claim 1 , wherein said polypeptide is derived from a member of the Actinomycetales.6Streptomyces. The polypeptide of any of the above claims claim 1 , wherein said polypeptide is derived from a member of the . spp.7Streptomyces rubiginosus.. The polypeptide of claim 6 , wherein said is8Streptomyces lividans.. The polypeptide of claim 6 , wherein said is9Streptomyces scabiei.. The polypeptide of claim 6 , wherein said is10. The polypeptide of any of the above claims claim 6 , wherein said polypeptide has protease activity.11. The polypeptide of claim 10 , wherein said protease activity comprises casein hydrolysis claim 10 , collagen hydrolysis claim 10 , elastin hydrolysis claim 10 , keratin hydrolysis claim 10 , soy protein hydrolysis or corn meal protein hydrolysis.12. The polypeptide of any of the above claims claim 10 , wherein said polypeptide retains at least 50% of its maximal activity between pH 4.5 and 9.5.13. The polypeptide of any of the above claims claim 10 , ...

PROTEASE VARIANTS HAVING AN IMPROVED WASHING PERFORMANCE

The disclosure relates to proteases, the amino acid sequence of which has been modified in particular with regard to the use thereof in detergents and cleaning agents, all sufficiently similar proteases having a corresponding modification and nucleic acids coding for them. The disclosure further relates to methods and uses of said proteases and to agents containing them, in particular detergents and cleaning agents. 11. A protease comprising an amino acid sequence which is identical to the amino acid sequence specified in SEQ ID NO. or SEQ ID NO. 2 over the total length thereof to an extent of at least about 70% , and which comprises the amino acid D at position 97 and/or the amino acid E at position 99 in the numbering according to SEQ ID NO. 1.2. The protease according to claim 1 , wherein claim 1 , in the numbering according to SEQ ID NO 1 claim 1 , said protease has one or more amino acid substitutions claim 1 , which are selected from N97D claim 1 , S97D claim 1 , R99E and S99E.3. The protease according to claim 1 , wherein its amino acid sequence corresponds to one of the amino acid sequences specified in SEQ ID NO. 4 to SEQ ID NO. 9.4. A method for producing a protease claim 1 , the method comprising the step of:introducing an amino acid substitution N97D and/or R99E in the numbering according to SEQ ID NO. 1 into a starting protease identical to the amino acid sequence specified in SEQ ID NO. 1 over the total length thereof to an extent of at least about 70%; orintroducing an amino acid substitution S97D and/or S99E in the numbering according to SEQ ID NO. 1 into a starting protease identical to that specified in SEQ ID NO. 2 over the total length thereof to an extent of at least 70%.5. (canceled)6. A nucleic acid coding for a protease according to .7. (canceled)8. (canceled)9. (canceled)10. The protease according to claim 1 , wherein the protease is utilized in an agent in an amount of from about 2 μg to about 20 mg per g of the agent.11. The protease ...

CYSTEINE PROTEASE

The present invention relates to a novel polypeptide which displays IgG cysteine protease activity, and in vivo and ex vivo uses thereof. Uses of the polypeptide include methods for the prevention or treatment of diseases and conditions mediated by IgG, and methods for the analysis of IgG. 1. A polypeptide having IgG cysteine protease activity and comprising a variant of the sequence of SEQ ID NO:2 , which variant:(a) is at least 50% identical to SEQ ID NO: 2;(b) has a cysteine (C) at the position in said variant sequence which corresponds to position 94 of SEQ ID NO: 1; and optionally(c) has, at the positions in said variant sequence which correspond to positions 84, 262, 284 and 286 of SEQ ID NO: 1, a lysine (K), a histidine (H), an aspartic acid (D) and an aspartic acid (D), respectively;wherein said polypeptide is more effective at cleaving IgG than IdeS and/or is less immunogenic than IdeS.2. A polypeptide according to claim 1 , wherein said variant of the sequence of SEQ ID NO: 2:(1) has a positively charged amino acid at the position in said variant which corresponds to position 130 of SEQ ID NO: 1, optionally wherein said positively charged amino acid is arginine (R) or lysine (K); and/or(2) has a positively charged amino acid at the position in said variant which corresponds to position 131 of SEQ ID NO: 1, optionally wherein said positively charged amino acid is arginine (R) or lysine (K); and/or(3) does not include the contiguous sequence NQTN; and/or(4) does not include the contiguous sequence DSFSANQEIR YSEVTPYHVT.3. A polypeptide according to claim 1 , wherein said variant of the sequence of SEQ ID NO: 2 is at least 80% claim 1 , 90% claim 1 , 95% or 99% identical to SEQ ID NO: 2.4. A polypeptide according to claim 1 , which comprises or consists of the sequence of any one of SEQ ID NOs: 3 to 16 claim 1 , optionally wherein said sequence includes an additional methionine at the N terminus and/or a histidine tag at the C terminus.5. A polypeptide ...

CLEANING AGENT CONTAINING PROTEASE AND AMYLASE

A cleaning agent, preferably a dishwasher detergent, preferably a hand dishwashing detergent, having at least one protease and at least one amylase as defined herein. The invention also relates to the use of the type of cleaning agent for cleaning solid surfaces and to a method for cleaning hard surfaces using the described cleaning agent. The invention further relates to the use of a specific enzyme combination as defined herein for improving the cleaning action of a cleaning agent. 1. A cleaning agent , characterized in that the cleaning agent comprises at least one protease and at least one amylase ,{'i': Bacilllus', 'Bacillus amyloliquefaciens, 'a) the amylase being a hybrid amylase from the mature α-amylase from sp. no. 707 and the mature α-amylase from or a functional fragment or a variant thereof, which has an amino acid sequence which is at least 80% identical to the amino acid sequence specified in SEQ ID NO:1 over the total length thereof; and'}{'i': 'Bacillus lentus', 'b) the at least one protease comprising the mature alkaline protease from DSM 5483 or a functional fragment or a variant thereof and having an amino acid sequence which is at least 80% identical to the amino acid sequence specified in SEQ ID NO:2 over the total length thereof and which optionally has at least one amino acid substitution at one, two, three, or four of the following positions 3, 4, 99, and 199 using the numbering according to SEQ ID NO:2.'}2. The cleaning agent according to claim 1 , characterized in that the at least one protease has the amino acid substitution R99E or R99D claim 1 , and additionally at least one or two of the amino acid substitutions S3T claim 1 , V4I claim 1 , and V199I.3. The cleaning agent according to claim 2 , characterized in that the at least one protease has the amino acid sequence according to SEQ ID NO:3.4. The cleaning agent according to claim 1 , characterized in thati. the at least one amylase and the at least one protease are used in a mass ...

Polypeptides Having Protease Activity

The present invention relates to isolated polypeptides having proteaseactivity and isolated polynucleotides encoding the polypeptides. The invention also relates to nucleic acid constructs, vectors, and host cells comprising the polynucleotides as well as methods of producing and using the polypeptidesin e.g. animal feed and detergents. 124-. (canceled)25. An isolated polypeptide having protease activity , selected from the group consisting of:(a) a polypeptide having at least 80% sequence identity to the polypeptide of SEQ ID NO: 5, SEQ ID NO: 6, or the mature polypeptide of SEQ ID NO: 2 or SEQ ID NO: 4; (i) the mature polypeptide coding sequence of SEQ ID NO: 1,', '(ii) the mature polypeptide coding sequence of SEQ ID NO: 3, or', '(iii) the full-length complementary strand of (i) or (ii);, '(b) a polypeptide encoded by a polynucleotide that hybridizes under high stringency conditions, or very high stringency conditions with'}(c) a polypeptide encoded by a polynucleotide having at least 80% sequence identity to the mature polypeptide coding sequence of SEQ ID NO: 1 or SEQ ID NO: 3;(d) a variant comprising a substitution, deletion, and/or insertion of one or more (several) amino acids of the polypeptide of SEQ ID NO: 5, SEQ ID NO: 6, or the mature polypeptide of SEQ ID NO: 2 or SEQ ID NO: 4; and(e) a fragment of a polypeptide of (a), (b), (c) or (d), that has protease activity.26. The polypeptide of claim 25 , having at least 90% sequence identity to SEQ ID NO: 5.27. The polypeptide of claim 25 , having at least 90% sequence identity to SEQ ID NO: 6.28. The polypeptide of claim 25 , having at least 90% sequence identity to the mature polypeptide of SEQ ID NO: 2.29. The polypeptide of claim 25 , having at least 90% sequence identity to the mature polypeptide of SEQ ID NO: 4.30. A composition comprising the polypeptide of .31. An animal feed additive comprising{'claim-ref': {'@idref': 'CLM-00025', 'claim 25'}, '(i) at least one polypeptide of ; and'}(ii) at least one ...

DETERGENT COMPOSITIONS COMPRISING SUBTILASE VARIANTS

The present invention relates to detergent compositions comprising subtilisin variants and methods for obtaining such detergent compositions. The present invention also relates to the use of such detergent compositions, especially in laundry or in hard surface cleaning applications. 1. A detergent composition comprising a subtilisin variant having protease activity , the variant comprising the substitutions corresponding to Y217X and N218Z of SEQ ID NO: 2 , wherein X and Z are selected from the group consisting of D , E , R , K , H , S and T , wherein when X is either K , H or R then Z is also selected from K , H or R and wherein when X is either D , E , S or T then Z is also selected from D , E , S or T.2. The detergent composition according to wherein X and Z in the variant are the same amino acid.3. The detergent composition according to wherein X and Z in the variant are D or E.4. The detergent composition according to wherein X and Z in the variant are K or R.5. The detergent composition of claim 1 , wherein the variant has at least about 60% but less than 100% sequence identity to the mature polypeptide of SEQ ID NO: 2 or 4.6. The detergent composition of claim 1 , wherein the variant consists of 150 to 350 amino acids.7. The detergent composition of claim 1 , wherein the number of alterations in the variant is 1-20 alterations.8. The detergent composition of claim 1 , wherein the variant comprises any one of the substitutions selected from the group consisting of [Y217D+N218D] claim 1 , [Y217E+N218E] claim 1 , [Y217D+N218E] claim 1 , [Y217E+N218D] claim 1 , [Y217E+N218S] claim 1 , [Y217S+N218E] claim 1 , [Y217S+N218S] claim 1 , [Y217D+N218S] claim 1 , [Y217S+N218D] claim 1 , [Y217E+N218T] claim 1 , [Y217T+N218E] claim 1 , [Y217T+N218T] claim 1 , [Y217D+N218T] claim 1 , [Y217T+N218D] [Y217K+N218K] claim 1 , [Y217R+N218R] claim 1 , [Y217K+N218R] claim 1 , [Y217R+N218K] claim 1 , [Y217R+N218H] claim 1 , [Y217H+N218R] claim 1 , [Y217H+N218H] claim 1 , [Y217K+ ...

COMPOSITIONS AND METHODS COMPRISING SERINE PROTEASE VARIANTS

The present invention provides methods for protein engineering and serine protease variants produced there from. Specifically, the present invention provides serine protease variants having one or more substitutions as compared to a reference serine protease. In addition, the present invention provides compositions comprising these serine protease variants. In some embodiments, the present invention provides cleaning compositions comprising at least one of these serine protease variants. 122-. (canceled)23BacillusB. amyloliquefaciens. An isolated subtilisin variant of a subtilisin , wherein said subtilisin variant is a mature form having proteolytic activity and at least 70% sequence identity to SEQ ID NO:2 , and , wherein said variant comprises a combination of substitutions selected from: TS87N/G118V/S128L/P129Q/S130A/S24W/S101L/Q109K , S87N/G118V/S128L/P129Q/S130A/N18K/G97P/S101L/Q109R/N185R/A215R , S87N/G118V/S128L/P129Q/S130A/172V/Q109R/S164I , S87N/G118V/S128L/P129Q/S130A/S101Y/Q109R/S188D/N248R , S87N/G118V/S128L/P129Q/S130A/N18K/G97P/S101Y/Q109L/N185R/A215R , S87R/G118R/S128L/P129Q/S130A/S101K/S188D/N248R , S87N/G118V/S128L/P129Q/S130A/S24W/S101L/Q109L , S87N/G118V/S128L/P129Q/S130A/N18K/G97P/S101Y/Q109R/N185R/A215R , S87N/G118V/S128L/P129Q/S130A/172V/S101L/Q109R/S164I , S87N/G118V/S128L/P129Q/S130A/S101Y/Q109R/S188D/T213E/N248R , S87R/G118R/S128L/P129Q/S130A/172V/S164I/S188D/N248R , S87N/G118V/S128L/P129Q/S130A/N76D , S87N/G118V/S128L/P129Q/S130A/S24W/S101Y/Q109K , S87N/G118V/S128L/P129Q/S130A/N43S/P52V/S101R/Q109R , S87N/G118V/S128L/P129Q/S130A/172V/S101Y/Q109R/S164I , S87N/G118V/S128L/P129Q/S130A/S101L/Q109L/S188D/N248R , S87N/G118V/S128L/P129Q/S130A/172V/Q109R/S164I/S188D/N248R , S87N/G118V/S128L/P129Q/S130A/N76D/S101L , S87N/G118V/S128L/P129Q/S130A/S24W/S101Y/Q109L , S87N/G118V/S128L/P129Q/S130A/N76D/S164I , S87R/G118R/S128L/P129Q/S130A/N76D/S188D/N248R , S87N/G118V/S128L/P129Q/S130A/S101Y/Q109L/S188D/N248R , S87R/G118R/S128L/P129Q/S130A/V118R/S188D/ ...

DESIGNED BIOSURFACTANTS, THEIR MANUFACTURE, PURIFICATION AND USE

The present invention relates to designed polypeptide biosurfactants that may be prepared by recombinant technology in commercially useful amounts and purified by simple non-chromatographic methods. The designed polypeptide biosurfactants comprise at least one stimuli-responsive amino acid residue or at least one glutamine or asparagine residue and may be useful in modulating the stability of a foam, alone or in combination with an α-helical peptide. The designed polypeptide biosurfactant may be useful in the formation and collapse of foams in foods, beverages, pharmaceuticals, personal care products, cosmetics, cleaning products, mineral recovery, bioremediation, oil recovery and laundry products. The designed biosurfactants may also be useful in recombinant production and purification of peptides, polypeptides and proteins. 175-. (canceled)76. A polypeptide or protein comprising at least two α-helical peptides linked by a linking sequence of 3 to 11 amino acid residues , wherein the protein or polypeptide has a folded tertiary structure with a hydrophobic core and a hydrophilic surface; and {'sub': 'n', '(a b c d d′ e f g)'}, 'wherein each α-helical peptide comprises a sequence of amino acid residueswherein n is an integer from 2 to 12;amino acid residues a and d are hydrophobic amino acid residues;amino acid residue d′ is absent or is a hydrophobic amino acid residue;at least one of amino acid residues b and c and at least one of amino acid residues e and f are hydrophilic amino acid residues, the other of amino acid residues b and c and e and f are any amino acid residue, provided that amino acid residues b and c are not both charged amino acid residues with the same charge and amino acid residues e and f are not both charged amino acid residues with the same charge;amino acid residue g is any amino acid residue; i) each α-helical peptide comprises at least one stimuli-responsive amino acid residue; or', 'ii) each sequence (a b c d d′ e f g) in the α-helical ...

Polypeptides Having Protease Activity and Polynucleotides Encoding Same

The present invention relates to isolated polypeptides having protease activity, and polynucleotides encoding the polypeptides. The invention further relates to the use of such polypeptides in detergent and/or in cleaning processes. The invention also relates to nucleic acid constructs, vectors, and host cells comprising the polynucleotides as well as methods of producing the polypeptides. 118-. (canceled)19. A recombinant host cell comprising a nucleic acid construct or expression vector comprising a polynucleotide encoding a polypeptide having protease activity , whereinthe polypeptide has at least 85% sequence identity to the mature polypeptide of SEQ ID NO: 2; at least 80% sequence identity to the mature polypeptide of SEQ ID NO: 4; or at least 89% sequence identity to the mature polypeptide of SEQ ID NO: 6; andthe polynucleotide is operably linked to one or more control sequences that direct the production of the polypeptide in the recombinant host cell.20. The recombinant host cell of claim 19 , wherein the polypeptide has at least 90% sequence identity to the mature polypeptide of SEQ ID NO: 2; the mature polypeptide of SEQ ID NO: 4; or the mature polypeptide of SEQ ID NO: 6.21. The recombinant host cell of claim 19 , wherein the polypeptide has at least 95% sequence identity to the mature polypeptide of SEQ ID NO: 2; the mature polypeptide of SEQ ID NO: 4; or the mature polypeptide of SEQ ID NO: 6.22. The recombinant host cell of claim 19 , wherein the polypeptide encoded by a polynucleotide having at least 85% sequence identity to the mature polypeptide coding sequence of SEQ ID NO: 1; a polynucleotide having at least 80% sequence identity to the mature polypeptide coding sequence of SEQ ID NO: 3; or a polynucleotide having at least 89% sequence identity to the mature polypeptide coding sequence of SEQ ID NO: 5.23. The recombinant host cell of claim 19 , wherein the polypeptide is a fragment of the mature polypeptide of SEQ ID NO: 2 claim 19 , 4 or 6.24. ...

AUTOMATIC DISHWASHING DETERGENT COMPOSITION

The present invention is in the field of automatic dishwashing detergent compositions, as well as methods of making and using same. In particular, it relates to an automatic dishwashing detergent composition comprising a new protease. The automatic dishwashing detergent composition provides improved cleaning and finishing. In particular the composition of the invention provides better proteinaceous removal at the same level of other proteases available in the market. This also alternatively allows for the use of a lower level of the protease of the invention and therefore a more cost effective composition. 2. The automatic dishwashing detergent composition according to wherein the builder comprises a phosphate or a non-phosphate builder and wherein the non-phosphate builder is selected from MGDA (methyl-glycine-diacetic acid); GLDA (glutamic-N claim 1 ,N-diacetic acid) claim 1 , IDS (iminodisuccinic acid) claim 1 , carboxy methyl inulin salts and derivatives thereof and a mixture thereof.3. The automatic dishwashing detergent composition according to further comprising a sulfonated polymer.4. The automatic dishwashing detergent composition according to further comprising a drying aid.5. The automatic dishwashing detergent composition according to further comprising an amylase enzyme.6. The automatic dishwashing detergent composition according to further comprising a cellulase enzyme.7. The automatic dishwashing detergent composition according to wherein the level of protease is from about 0.01 mg to about 5 mg of active protease per gram of composition.8. The automatic dishwashing detergent composition according to wherein the composition is in unit dose form and wherein the weight of the composition is from about 10 grams to about 25 grams.9. The automatic dishwashing detergent dosing element for use in an auto-dosing device the dosing element comprising a composition according to .10. A method of dishwashing in an automatic dishwashing machine using an automatic ...

PRODUCTION OF THERMOLYSIN AND VARIANTS THEREOF AND USE IN LIQUID DETERGENTS

The present invention provides methods and compositions comprising at least one thermolysin-like neutral protease enzyme with improved storage stability and/or catalytic activity. In some embodiments, the thermolysin finds use in cleaning and other applications comprising detergent. In some particularly preferred embodiments, the present invention provides methods and compositions comprising thermolysin formulated and/or engineered to resist detergent-induced inactivation. 14-. (canceled)5. An isolated thermolysin variant wherein said thermolysin has at least 95% amino acid identity with the amino acid sequence set forth in SEQ ID NO: 3.6. The thermolysin variant of claim 5 , wherein said thermolysin variant comprises the amino acid sequence set forth in SEQ ID NO: 3.7. (canceled)8Geobacillus. The isolated thermolysin variant of claim 5 , wherein said thermolysin variant is a thermolysin variant having an amino acid sequence comprising one or more substitutions at positions chosen from positions equivalent to positions 6 claim 5 , 7 claim 5 , 49 claim 5 , 56 claim 5 , 58 claim 5 , 61 claim 5 , 63 claim 5 , 65 claim 5 , 75 claim 5 , 128 claim 5 , 151 claim 5 , 156 claim 5 , 196 claim 5 , 273 claim 5 , 278 claim 5 , and 280 of the amino acid sequence set forth as SEQ ID NO: 3.9. (canceled)10Geobacillus. The isolated thermolysin variant of claim 5 , wherein said thermolysin variant is a thermolysin variant having an amino acid sequence comprising one or more substitutions at positions chosen from positions equivalent to positions 4 claim 5 , 6 claim 5 , 7 claim 5 , 36 claim 5 , 49 claim 5 , 53 claim 5 , 56 claim 5 , 58 claim 5 , 61 claim 5 , 63 claim 5 , 65 claim 5 , 75 claim 5 , 85 claim 5 , 108 claim 5 , 128 claim 5 , 129 claim 5 , 151 claim 5 , 156 claim 5 , 194 claim 5 , 195 claim 5 , 196 claim 5 , 261 claim 5 , 265 claim 5 , 273 claim 5 , 278 claim 5 , 280 and 297 of the amino acid sequence set forth as SEQ ID NO: 3.11. (canceled)12. The isolated thermolysin ...

Automatic Dishwashing Detergent Composition

A phosphate-free automatic dishwashing cleaning composition including: i) a protease wherein the protease is a variant of a parent protease having the amino acid sequence of SEQ ID NO:1 and the variant protease has at least 90% identity with the amino acid sequence of SEQ ID NO:1 wherein the protease comprises at least one aspartic acid residue in the active site loop region from position 95 to 103 (BPN′ numbering); and ii) more than 15% of organic complexing agent system comprising a weak complexing agent and a strong complexing agent in a weight ratio of from about 0.5:1 to about 2:1. 1. A phosphate-free automatic dishwashing cleaning composition comprising:i) a protease wherein the protease is a variant of a parent protease having the amino acid sequence of SEQ ID NO:1 and the variant protease has at least 90% identity with the amino acid sequence of SEQ ID NO:1 wherein the protease comprises at least one aspartic acid residue in the active site loop region from position 95 to 103 (BPN′ numbering); andii) more than 15% of organic complexing agent system comprising a weak complexing agent and a strong complexing agent in a weight ratio of from about 0.5:1 to about 2:1.2. A composition according to wherein the variant comprisesi) one or more of the amino acid substitutions selected from the group consisting of X95D, X96D, X97D, X98E, X99D, X100D, X101D, X102D and X103D versus SEQ ID NO:1; orii) one or more of the insertions selected from the group consisting of X95XD, X96XDE, X97XD, X98XD, X99XD, X100XD, X101XD, X102XD and X103XD versus SEQ ID NO:1; oriii) one or more of the amino acid substitutions selected from the group consisting of X95D, X96D, X97D, X98E, X99D, X100D, X101D, X102D and X103D versus SEQ ID NO:1, in combination with one or more of the insertions selected from the group consisting of X95XD, X96XDE, X97XD, X98XD, X99XD, X100XD, X101XD, X102XD and X103XD versus SEQ ID NO:1.3. A composition according to wherein the variant further comprises ...

Automatic Dishwashing Detergent Composition

A phosphate-free automatic dishwashing cleaning composition including a protease wherein the protease is a variant of a parent protease having the amino acid sequence of SEQ ID NO:1 and the variant protease has at least 90% identity with the amino acid sequence of SEQ ID NO:1 wherein the protease comprises at least one amino acid residue with a carboxylic acid side chain in the active site loop region from position 95 to 103 (BPN′ numbering) with the proviso that the variant protease does not have 100% identity with SEQ ID NO:3, SEQ ID NO:4, or SEQ ID NO: 5. 1. A phosphate-free automatic dishwashing cleaning composition comprising a protease wherein the protease is a variant of a parent protease having the amino acid sequence of SEQ ID NO:1 and the variant protease has at least 90% identity with the amino acid sequence of SEQ ID NO:1 wherein the protease comprises at least one amino acid residue with a carboxylic acid side chain in the active site loop region from position 95 to 103 (BPN′ numbering) with the proviso that the variant protease does not have 100% identity with SEQ ID NO:3 , SEQ ID NO:4 , or SEQ ID NO: 5.2. A composition according to wherein the variant comprisesi) one or more of the amino acid substitutions selected from the group consisting of X95{D,E}, X96{D,E}, X97{D,E}, X98{D,E}, X99{D,E}, X100{D,E}, X101{D,E}, X102{D,E} and X103{D,E} versus SEQ ID NO:1; orii) one or more of the insertions selected from the group consisting of X95X{D,E}, X96X{D,E}, X97X{D,E}, X98X{D,E}, X99X{D,E}, X100X{D,E}, X101X{D,E}, X102X{D,E} and X103X{D,E} versus SEQ ID NO:1; oriii) one or more of the amino acid substitutions selected from the group consisting of X95{D,E}, X96{D,E}, X97{D,E}, X98{D,E}, X99{D,E}, X100{D,E}, X101{D,E}, X102{D,E} and X103{D,E} versus SEQ ID NO:1 in combination with one or more of the insertions selected from the group consisting of X95X{D,E}, X96X{D,E}, X97X{D,E}, X98X{D,E}, X99X{D,E}, X100X{D,E}, X101X{D,E}, X102X{D,E} and X103X{D,E} versus ...

Automatic Dishwashing Detergent Composition

A phosphate-free automatic dishwashing cleaning composition including a protease wherein the protease is a variant of a parent protease having the amino acid sequence of SEQ ID NO:1 and the variant protease has at least 90% identity with the amino acid sequence of SEQ ID NO:1 wherein the protease includes at least one glutamic acid residue in the active site loop region from position 95 to 103 (BPN′ numbering).

Proteases With Modified Pro Regions

The present invention provides methods and compositions for the production of mature proteases in bacterial host cells. The compositions include modified polynucleotides that encode modified proteases, which have at least one mutation in the pro region; the modified serine proteases encoded by the modified polynucleotides; expression cassettes, DNA constructs, and vectors comprising the modified polynucleotides that encode the modified proteases; and the bacterial host cells transformed with the vectors of the invention. The methods include methods for enhancing the production of mature proteases in bacterial host cells e.g. sp. host cells. The produced proteases find use in the industrial production of enzymes, suitable for use in various industries, including but not limited to the cleaning, animal feed and textile processing industry. 1. An isolated modified polynucleotide encoding a modified protease , said isolated modified polynucleotide comprising a first polynucleotide encoding a signal peptide , said first polynucleotide being operably linked to a second polynucleotide encoding the pro region set forth in SEQ ID NO:7 , wherein said pro region comprises a combination of substitutions of at least two amino acids at positions chosen from positions 6 , 30 and 32 of said pro region , said second polynucleotide being operably linked to a third polynucleotide encoding the mature region of a protease that is at least about 60% identical to the mature protease of SEQ ID NO: 11.2Bacillus clausiiBacillus lentus.. The isolated modified polynucleotide of claim 1 , wherein said mature protease is a wild-type or variant alkaline serine protease derived from or3. The isolated modified polynucleotide of claim 1 , wherein said mature protease has an amino acid sequence chosen SEQ ID NOS: 9 claim 1 , 11 claim 1 , 13 claim 1 , 15 claim 1 , 17 claim 1 , 19 claim 1 , and 21.4. The isolated polynucleotide of claim 1 , wherein said signal peptide has an amino acid sequence chosen ...

PERFORMANCE-ENHANCED AND TEMPERATURE-RESISTANT PROTEASE VARIANTS

Proteases that comprise an amino acid sequence that is at least 70% identical to the amino acid sequence indicated in SEQ ID NO. 1 over its entire length and that comprise, in the count in accordance with SEQ ID NO. 1, the amino acid substitution R99D in combination with at least two further amino acid substitutions that are selected from the group consisting of S3T, V4I, and V199I, display very good cleaning performance in particular on blood-containing stains, as well as very good temperature stability. 1. A protease for use in washing and cleaning agents comprising a protease variant having an amino acid sequence that is at least 90% identical to the amino acid sequence indicated in SEQ ID NO. 1 over its entire length and wherein , in the count in accordance with SEQ ID NO. 1 , the protease variant has the amino acid substitution R99D and at least two further amino acid substitutions selected from the group consisting of S3T , V4I , and V199I.2. A protease , selected from the group consisting of proteases obtainable from:{'claim-ref': {'@idref': 'CLM-00001', 'claim 1'}, '(a.) a protease according to as a starting molecule by single or multiple conservative amino acid substitution, wherein the protease comprises, in the count in accordance with SEQ ID NO. 1, the amino acid substitution R99D in combination with at least two further amino acid substitutions that are selected from the group consisting of S3T, V4I, and V199I;'}{'claim-ref': {'@idref': 'CLM-00001', 'claim 1'}, '(b.) a protease according to as a starting molecule by fragmentation, deletion mutagenesis, insertion mutagenesis, or substitution mutagenesis, and comprises an amino acid sequence that corresponds to the starting molecule over a length of at least 50, 60, 70, 80, 90, 100, 110, 120, 130, 140, 150, 160, 170, 180, 190, 200, 210, 220, 230, 240, 250, 260, 265, or 266 continuously connected amino acids, wherein the amino acid substitution R99D contained in the starting molecule, in combination with ...

ENZYME BASED PRODUCTS FOR CAR WASHES

The present invention relates to a liquid composition soluble in water or other polar substance and its use for vehicle cleansing and care, in particular for all the treatments provided in the washing steps of vehicles. 1. A method for washing a vehicle , said method comprising:providing a composition including an enzymatic component; andwashing said vehicle with said composition.2. The method as in claim 1 , wherein said composition is liquid and comprises a detergent.3. The method as in claim 1 , wherein said washing comprises diluting said composition with water by pumping said water in an automated car wash station and introducing said diluted composition to contact said vehicle in said automated car wash station.4. The method as in claim 1 , wherein said composition is a liquid detergent and includes a first enzymatic component claim 1 , andfurther comprising, after said washing, introducing a further composition being a liquid and including a second enzymatic component, to contact said vehicle along with wax, said first enzymatic component differing from said second enzymatic component.5. The method as in claim 1 , wherein said enzymatic component is present in a concentration between 1% and 10% by weight.6. The method as in claim 5 , wherein said composition comprises a detergent and further includes surfactants and ethanol.7. The method as in claim 1 , wherein said composition comprises a detergent and said enzymatic component comprises an amylase.8. The method as in claim 1 , wherein said composition comprises a detergent and enzymatic component comprises a protease.9. The method as in claim 1 , wherein said enzymatic component comprises a lipase.10. The method as in claim 1 , wherein said vehicle is an automobile claim 1 , said enzymatic component is a microorganism.11. A method for washing a vehicle in an automated car wash claim 1 , said method comprising:providing a composition including an enzymatic component;delivering said composition to a vehicle in ...

Powder Detergent Compositions

The invention relates to moderate pH and optionally low conductivity powder detergent compositions comprising a protease. 1. A powder detergent composition comprising a protease and at least one detergent component , wherein the composition has a pH of not more than about 9 , wherein pH is determined in a 5 g/l solution of the composition in deionized water at 20° C.2. The composition of claim 1 , wherein the composition has a conductivity of not more than about 4.0 mS/cm claim 1 , wherein conductivity is determined in a 5 g/l solution of the composition in deionized water at 20° C.3. The composition of claim 1 , wherein the composition has a pH determined as defined in of a) from about 7.0 to not more than about 9.0 claim 1 , for example from about 7.2 to about 8.9 claim 1 , such as from about 7.4 to about 8.8 claim 1 , such as from about 7.6 to about 8.7 claim 1 , such as from about 7.8 to about 8.6; b) from about 7.0 to about 8.2 claim 1 , such as from about 7.2 to about 8.0; or c) from about 7.8 to about 8.8 claim 1 , such as from about 8.0 to about 8.6.4. The composition of claim 2 , wherein the composition has a conductivity of not more than about 3.9 mS/cm claim 2 , such as not more than about 3.8 mS/cm claim 2 , such as not more than about 3.7 mS/cm claim 2 , such as not more than about 3.6 mS/cm claim 2 , such as not more than about 3.5 mS/cm claim 2 , such as not more than about 3.4 mS/cm claim 2 , such as not more than about 3.3 mS/cm claim 2 , such as not more than about 3.2 mS/cm claim 2 , such as not more than about 3.1 mS/cm claim 2 , such as not more than about 3.0 mS/cm claim 2 , such as not more than about 2.8 mS/cm claim 2 , such as not more than about 2.6 mS/cm claim 2 , such as not more than about 2.4 mS/cm claim 2 , such as not more than about 2.2 mS/cm claim 2 , or not more than about 2.0 mS/cm.5. The composition of claim 1 , wherein the protease is selected from the group consisting of:a) a variant of the polypeptide of SEQ ID NO: 1, wherein ...

PROTEASE VARIANTS AND POLYNUCLEOTIDES ENCODING SAME

The present invention relates to protease variants and methods for obtaining protease variants. The present invention also relates to polynucleotides encoding the variants; nucleic acid constructs, vectors, and host cells comprising the polynucleotides; and methods of using the variants. 1. A protease variant having at least 86% sequence identity to SEQ ID NO: 3 and having an amino acid substitution at position S173 , wherein the variant has protease activity.2. The protease variant of claim 1 , wherein the substitution at position S173 is S173P or S173Y.3. The protease variant of claim 1 , further comprising a substitution at one or more positions corresponding to positions S171 claim 1 , S175 claim 1 , G179 and F180.4. The protease variant of claim 3 , wherein the substitution at position S171 is S171W claim 3 , S171K claim 3 , S171E or S171N.5. The protease variant of claim 3 , wherein the substitution at position S175 is S175A claim 3 , S175V or S175P.6. The protease variant of claim 3 , wherein the substitution at position G179 is G179C claim 3 , G179V claim 3 , G179Q claim 3 , G179S claim 3 , G179T claim 3 , G179E claim 3 , G179H claim 3 , G179K claim 3 , G179M claim 3 , G179N claim 3 , G179Y or G179A.7. The protease variant of claim 3 , wherein the substitution at position F180 is F180Y.8. The protease variant of claim 1 , further comprising at least one amino acid substitution selected from the group consisting of Y39D; T40{D claim 1 ,P}; Q70N; T74M; L81{F claim 1 ,H claim 1 ,V}; A102T; 1121{V claim 1 ,T}; G132 {I claim 1 ,E}; 1137{M;E}; S144{Q claim 1 ,R}; D155N; G159S; V162R; G174{S claim 1 ,T}; N176G; T177S; T241P; 1247M; H256F;S2741; V286Q; and T297P.9. The protease variant of claim 1 , wherein said protease variant comprises any of the following sets of amino acid substitutions:S173P S274II137M S173PS171N S173PL81F S173PL81H S173PA102T S173PS144Q S173PI137E S173PS173P S175P F180YS173Y G174S S175A F180YS173P G174T S175V T177S F180YS173P G174K S175P N176G ...

Block Copolymer Complex Coacervate Core Micelles for Enzymatic Catalysis in Organic Solvent

Disclosed are complex coacervate core micelles comprising an enzyme capable of hydrolyzing organophosphorus compounds, such as nerve agents, and, for example, their use in remediation or decontamination of stockpiles of chemical weapons. 1. A nanostructure comprising: a block copolymer; and', 'an enzyme; or, 'a polyanionic polymer;'} 'a modified enzyme.', '(ii) a block copolymer; and'}6. The nanostructure of claim 1 , wherein the enzyme or modified enzyme is an organophosphate hydrolase or a modified organophosphate hydrolase.7. The nanostructure of claim 1 , wherein the enzyme or modified enzyme is an organophosphate acid anhydrolase or a modified organophosphate acid anhydrolase.8. The nanostructure of claim 1 , wherein the nanostructure is a nanostructure of form (i);and the polyanionic polymer is polyacrylic acid.9. The nanostructure of claim 1 , wherein the nanostructure is a nanostructure of form (ii);and the modified enzyme comprises at least one non-natural pendant anionic moiety.10. The nanostructure of claim 9 , wherein the pendant anionic moiety is covalently bonded to a lysine residue.11. The nanostructure of claim 9 , wherein the pendant anionic moiety is a carboxylate moiety.12. The nanostructure of claim 1 , wherein the nanostructure further comprises an aqueous liquid.13. The nanostructure of claim 12 , wherein the aqueous liquid comprises a buffer.14. The nanostructure of claim 13 , wherein the concentration of buffer in the aqueous liquid is about 10 mM to about 100 mM.15. The nanostructure of claim 12 , wherein the pH of the aqueous liquid is about 6.5 claim 12 , about 7.0 claim 12 , about 7.5 claim 12 , about 8.0 claim 12 , about 8.5 claim 12 , about 9.0 claim 12 , or about 9.5.16. A composition comprising:{'claim-ref': {'@idref': 'CLM-00001', 'claim 1'}, 'an organic phase, an aqueous liquid phase, and a plurality of nanostructures of .'}17. The composition of claim 16 , wherein the organic phase comprises claim 16 , consists essentially of claim ...

STABILIZED CELLULASE VARIANTS

Disclosed are variants of a cellulase having improved stability in the presence of a protease, and the use of such variants in laundry. 1. A variant having endoglucanase activity , where the variant has at least 80% sequence identity to the endoglucanase having SEQ ID NO: 1 , and where the variant has improved stability in an aqueous composition comprising a protease in comparison with the endoglucanase having the sequence of SEQ ID NO: 1.2. A variant having endoglucanase activity , where the variant has at least 80% sequence identity to the endoglucanase having SEQ ID NO: 2 , SEQ ID NO: 3 or SEQ ID NO: 4 , and where the variant has improved stability in an aqueous composition comprising a protease in comparison with the endoglucanase having the sequence of SEQ ID NO: 2 , SEQ ID NO: 3 , or SEQ ID NO: 4.3. A variant having endoglucanase activity , wherein the variant has at least 80% sequence identity to amino acids 1 to 212 of SEQ ID NO: 1 or amino acids 1 to 216 of SEQ ID NO: 1 , amino acids 1 to 211 of SEQ ID NO: 2 or amino acids 1 to 212 of SEQ ID NO: 2 , amino acids 1 to 211 of SEQ ID NO: 3 or amino acids 1 to 210 of SEQ ID NO: 3 , amino acids 1 to 211 of SEQ ID NO: 4.4. The variant of claim 1 , wherein the variant has a residual activity ratio (RAR) where the RAR is increased with at least 2 times the standard deviation for the assay.5. The variant of claim 1 , wherein the variant has a RAR of at least 1.1.6. The variant of claim 1 , wherein the variant comprises a substitution in comparison with the polypeptide having SEQ ID NO: 1 claim 1 , in one of more positions corresponding to the positions of SEQ ID NO: 1 of: 4 claim 1 , 6 claim 1 , 25 claim 1 , 32 claim 1 , 37 claim 1 , 41 claim 1 , 44 claim 1 , 51 claim 1 , 56 claim 1 , 77 claim 1 , 80 claim 1 , 82 claim 1 , 83 claim 1 , 85 claim 1 , 91 claim 1 , 93 claim 1 , 94 claim 1 , 96 claim 1 , 98 claim 1 , 100 claim 1 , 101 claim 1 , 103 claim 1 , 104 claim 1 , 114 claim 1 , 117 claim 1 , 118 claim 1 , 132 ...

Biotech Washing Agent

A natural biotech washing agent for the environment, which is truly natural and environment friendly, for removing oil stains and dirt on a clothing object and degrading the oil and dirt at the same time without using any powered tools, comprising a composition by percentage weight containing 0.5% marine alkaloids, 6.5-9.5% surfactant and 2.5-3.5% enzymes as active ingredients. The biotech washing agent is truly meant for the environment in that the composition is natural, the cleaning process is natural and energy-saving, the cleaning effect is great, the end products after cleaning is natural and cause no harm to the environment, and no powered tools is required to achieve the cleaning effect. In addition, the wastewater after the washing process of the present invention can continue to provide a cleaning effect to the sewage and the wastewater. 1. A biotech washing agent for washing an object for cleaning , comprising a composition by percentage weight containing 0.5% marine alkaloids , 6.5-9.5% surfactant and 2.5-3.5% enzymes as active ingredients.2. The biotech washing agent according to claim 1 , wherein the composition by percentage weight comprises 0.5% marine alkaloids claim 1 , 6.5% surfactant claim 1 , 2.5% enzymes and 90.5% deionized water claim 1 , wherein the marine alkaloids claim 1 , the surfactant and the enzymes are natural in nature.3. The biotech washing agent according to claim 2 , wherein the surfactant is composed of 2.5% anionic surfactants and 4% non-ionic surfactants and the surfactant is derived from coconut oil.4. The biotech washing agent according to claim 1 , wherein the enzymes is selected from the group consisting of lipase claim 1 , protease claim 1 , cellulase and amylase.5. The biotech washing agent according to claim 3 , wherein the enzymes is selected from the group consisting of lipase claim 3 , protease claim 3 , cellulase and amylase.6. The biotech washing agent according to claim 4 , wherein the enzymes comprises lipase ...

Polypeptides Having Cellobiohydrolase I Activity and Polynucleotides Encoding Same

The present invention relates to polypeptides having cellobiohydrolase I activity and polynucleotides having a nucleotide sequence which encodes for the polypeptides. The invention also relates to nucleic acid constructs, vectors, and host cells comprising the nucleic acid constructs as well as methods for producing and using the polypeptides.

Polypeptides Having Protease Activity

The present invention relates to isolated polypeptides having protease activity and isolated polynucleotides encoding the polypeptides. The invention also relates to nucleic acid constructs, vectors, and host cells comprising the polynucleotides as well as methods of producing and using the polypeptides in e.g. animal feed and detergents. 1. An isolated polypeptide having protease activity , selected from the group consisting of:(a) a polypeptide having at least 85% sequence identity to the mature polypeptide of SEQ ID NO: 2 and/or SEQ ID NO: 4; (i) the mature polypeptide coding sequence of SEQ ID NO: 1, and/or', '(ii) the mature polypeptide coding sequence of SEQ ID NO: 3, or', '(iii) the full-length complementary strand of (i) or (ii);, '(b) a polypeptide encoded by a polynucleotide that hybridizes under high stringency conditions, or very high stringency conditions with'}(c) a polypeptide encoded by a polynucleotide having at least 86% sequence identity to the mature polypeptide coding sequence of SEQ ID NO: 1 or SEQ ID NO: 3; and/or(d) a variant comprising a substitution, deletion, and/or insertion of one or more (several) amino acids of the mature polypeptide of SEQ ID NO: 2; and/or SEQ ID NO: 4.27-. (canceled)8. An isolated polynucleotide encoding the polypeptide of .9. A nucleic acid construct or expression vector comprising the polynucleotide of operably linked to one or more (several) control sequences that direct the production of the polypeptide in an expression host cell.10. A recombinant expression host cell comprising a polynucleotide of operably linked to one or more control sequences that direct the production of the polypeptide.11. A method of producing the polypeptide of claim 1 , comprising:(a) cultivating a cell, which in its wild-type form produces the polypeptide, under conditions conducive for production of the polypeptide; and(b) recovering the polypeptide.12. A method of producing the polypeptide having protease activity claim 1 , comprising ...

COMPOSITIONS AND METHODS FOR HANDLING POTENTIAL PRION CONTAMINATION

A composition and method of treatment for handling potential prion contamination of surfaces is disclosed. The products include and the treatment uses products that include at least one prion digester enzyme selected from a serine protease in solution with a non-ionic surfactant, a hydrotrope and high purity water 1. A composition comprising(a) at least one prion digester enzyme selected from the group of serine proteases selected from the group consisting of akalase, savinase, and mixtures thereof;(b) optionally one or more additional proteases that are not prion digester enzymes;(c) optionally a further enzyme selected from the group consisting of one or more lipases; one or more amylases, one or more cellulases and mixtures thereof;(d) a surfactant portion consisting essentially of non-ionic surfactant;{'sub': '6-10', '(e) optionally a hydrotrope consisting essentially of an alkali metal salt of a sulfated (unsubstituted or mono or di lower alkyl substituted) Caryl;'}(f) optionally calcium chloride;(g) optionally propylene glycol;(h) optionally a preservative;(i) optionally buffer;(j) high purity water;having a pH in the range of about 8 about 10;said at least one prion digester enzyme in an amount selected from about 0.01% by weight to about 15 % by weight based on the complete composition sufficient to degrade a prion material to non-infectious fragments after an exposure time selected from time periods within the range of about 10 minutes to about 30 minutes at a temperature selected from temperatures within the range of 45°°C. to 65° C.2. The method of wherein said at least one additional enzyme which is not a protease enzyme is present3. The method of wherein said at least one hydrotrope is present.4. The method of wherein said hydrotrope is selected from the group consisting of sodium xylene sulfonate claim 3 , sodium toluene sulfonate claim 3 , Dowfax claim 3 , sodium cumene sulfonate.5. The method of wherein said buffer is present and is selected from the ...

Automatic dishwashing detergent composition

An automatic dishwashing detergent composition comprising: a. at least 0.1 mg of active protease per gram of composition, wherein the protease is a variant of a protease that has at least 70% identity with the amino acid sequence of SEQ ID NO:1. wherein said variant comprise variations in one or more of the following positions: 32, 33, 48-54, 58-62, 94-107, 116, 123-133, 150, 152-156, 158-161, 164, 169, 175-186, 197, 198, 203-216 as compared with the protease in SEQ ID NO:1; and b. at least 0.05 mg of an active low temperature amylase per gram of composition.

NOVEL WHITENING AGENTS FOR CELLULOSIC SUBSTRATES

This invention relates to novel whitening agents for cellulosic substrates. The whitening agents are comprised of at least two components: at least one chromophore component and at least one polymeric component. Suitable chromophore components generally fluoresce blue, red, violet, or purple color when exposed to ultraviolet light, or they may absorb light to reflect these same shades. The whitening agents are further characterized by having a dispersion component value of the Hansen Solubility Parameter of less than or equal to about 17 MPa. This invention also relates to laundry care compositions including but not limited to liquid and/or powder laundry detergent formulations and rinse added fabric softening (RAFS) compositions that comprise such whitening agents.

Subtilase Variants And Polynucleotides Encoding Same

The present invention relates to novel subtilase variants exhibiting increased stability and preferably on par or improved wash performance. The variants of the invention are suitable for use in e.g. cleaning or detergent compositions, such as laundry detergent compositions and dish wash compositions, including automatic dish wash compositions. The present invention also relates to isolated DNA sequences encoding the variants, expression vectors, host cells, and methods for producing and using the variants of the invention.

IMPROVED CLEANING PERFORMANCE ON PROTEIN SENSITIVE SOILINGS VI

Proteases may include an amino acid sequence having at least 70% sequence identity with the amino acid sequence given in SEQ ID NO:1 over its entire length and, in each case based on the numbering according to SEQ ID NO:1. The protease may have (i) amino acid substitutions, such as 9T, 133A, 144K, 252T and 271E, at the positions corresponding to positions 9, 133, 144, 252 and 271; and (ii) at least one further amino acid substitution at at least one of the positions corresponding to positions 3, 4, 82, 156, 162 or 218. The production and use of said proteases help to improve cleaning performance. 1. A protease comprising an amino acid sequence having at least 70% sequence identity with the amino acid sequence given in SEQ ID NO:1 over its entire length , in each case based on the numbering according to SEQ ID NO:1 , wherein the protease comprises:amino acid substitutions at the positions corresponding to positions 9, 133, 144, 252, and 271; andat least one further amino acid substitution at at least one of the positions corresponding to positions 3, 4, 82, 156, 162, 218, and combinations thereof.2. The protease according to claim 2 , wherein the protease further has an additional amino acid substitution at the position corresponding to position 130.3. A protease comprising an amino acid sequence which has at least 70% sequence identity with the amino acid sequence given in SEQ ID NO:1 over its entire length claim 2 , in each case based on the numbering according to SEQ ID NO:1 claim 2 , wherein the protease comprises:(A) at least one amino acid substitution at at least one of the positions corresponding to positions 3, 4, 218, and combinations thereof; and/or(B) at least one amino acid substitution selected from 156D and 162I at at least one of the positions corresponding to positions 156 and 162.4. The protease according to claim 1 , wherein:the amino acid substitution at the position corresponding to position 3 is selected from the group consisting of 3K, 3A, 3R, ...

AUTOMATIC DISHWASHING COMPOSITION

A phosphate-free automatic dishwashing cleaning composition including a partially decarboxylated polyitaconic acid homopolymer. 1. A phosphate-free automatic dishwashing cleaning composition comprising a partially decarboxylated polyitaconic acid homopolymer.2. A composition according to wherein the level of decarboxylation of the polyitaconic acid homopolymer is at or above 40 mole % of carbon dioxide evolved per molar equivalent of itaconic acid in said homopolymer based upon a maximum level of decarboxylation of 200 mole %.3. A composition according to wherein the level of decarboxylation of the polyitaconic acid homopolymer is in the range of about 40 mole % to about 150 mole % of carbon dioxide evolved per molar equivalent of itaconic acid in said homopolymer based upon a maximum level of decarboxylation of 200 mole %.4. A composition according to wherein the level of decarboxylation of the polyitaconic acid homopolymer is in the range of about 50 mole % to about 90 mole % of carbon dioxide evolved per molar equivalent of itaconic acid in said homopolymer based upon a maximum level of decarboxylation of 200 mole %.5. A composition according to wherein the average molecular weight of the decarboxylated polyitaconic acid homopolymer is from about 800 g/mole to about 5 claim 1 ,000 g/mole.6. A composition according to wherein the composition comprises from about 0.1 to about 5% by weight of the composition of the polyitaconic acid homopolymer.7. A composition according to comprising a complexing agent selected from the group consisting of citric acid claim 1 , its salts and derivatives thereof claim 1 , methyl glycine diacetic acid claim 1 , its salts and derivatives thereof claim 1 , glutamic-N claim 1 ,N-diacetic acid claim 1 , its salts and derivatives thereof claim 1 , iminodisuccinic acid claim 1 , its salts and derivatives thereof claim 1 , carboxy methyl inulin claim 1 , its salts and derivatives thereof claim 1 , and mixtures thereof.8. A composition ...

SYSTEMS AND METHODS FOR EVOLVING ENZYMES WITH DESIRED ACTIVITIES

The present invention provides a new method for engineering or evolving enzymes to have desirable characteristics. Among the desirable characteristics is the ability to control catalytic activity through the use of a trigger molecule that rescues a catalytic site defect introduced during the engineering process. The method includes co-evolving enzyme and substrate to retain or improve substrate binding activity in the absence of catalytic activity. 128-. (canceled)29. An engineered enzyme that is competent for substrate binding but defective for substrate catalysis in the absence of an exogenous trigger molecule , said enzyme having the following characteristics:a mutation at a residue that is involved in the catalytic activity of the enzyme, which reduces or abolishes the catalytic activity of the enzyme for a chosen substrate, wherein the catalytic activity of the mutant enzyme can be restored by the exogenous trigger molecule; andanother mutation in the mutant enzyme, wherein the other mutation increased the catalytic activity, specificity, or both, of the mutant enzyme for a pre-selected substrate in the presence of the trigger molecule.30. The engineered enzyme of claim 29 , wherein the chosen substrate and the pre-selected substrate are different substrates.31. The engineered enzyme of claim 29 , wherein the engineered enzyme is a protease.32. The engineered enzyme of claim 31 , wherein the engineered enzyme is a serine protease.33. The engineered enzyme of claim 32 , wherein the serine protease is subtilisin.34. A composition comprising:{'claim-ref': {'@idref': 'CLM-00029', 'claim 29'}, 'the engineered enzyme of ; and at least one other substance that is compatible with the catalytic activity of the engineered enzyme.'}35. The composition of claim 34 , wherein the other substance is a trigger molecule that restores the catalytic activity of the engineered enzyme. This application is a Divisional Application of U.S. patent application Ser. No. 13/497,753, ...

Method for Improving Solubility of Alkaline Protease

Providing an alkaline protease exhibiting an improved solubility in a liquid detergent. A mutant alkaline protease consisting of the amino acid sequence represented by SEQ ID No: 2 or an amino acid sequence having 80% or more sequence identity therewith, in which at least one amino acid residue selected from the group consisting of the amino acid residues at predetermined positions of the amino acid sequence represented by SEQ ID No: 2 or corresponding positions thereto are substituted. 27.-. (canceled)8. The method according to claim 1 , wherein the liquid detergent is a concentrated liquid detergent comprising 40 to 90 mass % of a surfactant.1015.-. (canceled)16. A gene encoding the mutant alkaline protease according to .17. A recombinant vector comprising the gene according to .18. A transformant comprising the recombinant vector according to .19. A method for producing a mutant alkaline protease using the transformant according to .20. A liquid detergent composition comprising the mutant alkaline protease according to .21. The method according to claim 8 , wherein the identity is 90% or more.22. The method according to claim 8 , wherein the amino acid residues at position 30 claim 8 , position 68 and position 255 of the amino acid sequence represented by SEQ ID No: 2 or the corresponding positions thereto are the amino acid residues shown below:Position 30 or the corresponding position thereto: aspartic acid;Position 68 or the corresponding position thereto: histidine; andPosition 255 or the corresponding position thereto: serine.24. The method according to claim 8 , wherein the at least one amino acid residue comprises at least one amino acid residue selected from the group consisting of the amino acid residues at (A) position 405 claim 8 , (B) position 81 claim 8 , (C) position 40 claim 8 , (D) position 191 and (E) position 59 claim 8 , or positions corresponding thereto.25. The method according to claim 8 , wherein the at least one amino acid residue ...

USE AND PRODUCTION OF STORAGE-STABLE NEUTRAL METALLOPROTEASE

The present invention provides methods and compositions comprising at least one neutral metalloprotease enzyme that has improved storage stability. In some embodiments, the neutral metalloprotease finds use in cleaning and other applications. In some particularly preferred embodiments, the present invention provides methods and compositions comprising neutral metalloprotease(s) obtained from sp. In some more particularly preferred embodiments, the neutral metalloprotease is obtained from . In still further preferred embodiments, the neutral metalloprotease is a variant of the neutral metalloprotease. In yet additional embodiments, the neutral metalloprotease is a homolog of the neutral metalloprotease. The present invention finds particular use in applications including, but not limited to cleaning, bleaching and disinfecting. 112-. (canceled)13Bacillus. An isolated neutral metalloprotease variant having at least 95% sequence identity to and having an amino acid sequence comprising at least one substitution of an amino acid made at a position equivalent to a position in a neutral metalloprotease comprising the amino acid sequence set forth in SEQ ID NO: 18.14. The isolated neutral metalloprotease variant of claim 13 , wherein said substitutions are made at positions equivalent to positions 1 claim 13 , 3 claim 13 , 4 claim 13 , 5 claim 13 , 6 claim 13 , 11 claim 13 , 12 claim 13 , 13 claim 13 , 14 claim 13 , 16 claim 13 , 21 claim 13 , 23 claim 13 , 24 claim 13 , 25 claim 13 , 31 claim 13 , 32 claim 13 , 33 claim 13 , 35 claim 13 , 36 claim 13 , 38 claim 13 , 44 claim 13 , 45 claim 13 , 46 claim 13 , 47 claim 13 , 48 claim 13 , 49 claim 13 , 50 claim 13 , 51 claim 13 , 54 claim 13 , 55 claim 13 , 58 claim 13 , 59 claim 13 , 60 claim 13 , 61 claim 13 , 62 claim 13 , 63 claim 13 , 65 claim 13 , 66 claim 13 , 69 claim 13 , 70 claim 13 , 76 claim 13 , 85 claim 13 , 86 claim 13 , 87 claim 13 , 88 claim 13 , 90 claim 13 , 91 claim 13 , 92 claim 13 , 96 claim 13 , 97 claim ...

Use of Amylase Variants at Low Temperature

The present invention relates to the use of alpha-amylase variants having improved activity relative to the parent enzyme at low temperature, including improved washing and/or dishwashing performance and/or increased stability at low temperature. The invention further relates a method for doing laundry, dish wash and/or cleaning such as institutional cleaning and to compositions for use at low temperature. 1. Use in a starch removing process of a variant or a variant of a parent alpha-amylase , wherein said variant comprises a deletion at one or more positions corresponding to positions selected from the group consisting of 180 , 181 , 182 , 183 and 184 of the mature polypeptide of SEQ ID NO 3 , wherein said variant having at least one improved property compared to an alpha-amylase having the identical amino acid sequence of said variant but not having the deletion at one or more of said positions , or compared to the parent alpha-amylase or compared to an alpha-amylase having the amino acid sequence shown in SEQ ID NO 4 and wherein the temperature in the starch removing process is below 40 deg C. , such as below 35 deg C.2. Use in laundry , dish wash , industrial or institutional cleaning of a variant or a variant of a parent alpha amylase , comprising a deletion at one or more positions corresponding to positions selected from the group comprising 180 , 181 , 182 , 183 and 184 of the mature polypeptide of SEQ ID NO 3 , wherein said variant having at least one improved property compared to an alpha-amylase having the identical amino acid sequence of said variant but not having the deletion at one or more of said positions , or compared to the parent alpha amylase or compared to SEQ ID NO 4 and wherein the temperature in laundry , dish wash , industrial and institutional cleaning is below 40 deg C. , such as below 35 deg C.3. The use according to claim 1 , wherein the starch removing process or the cleaning process is performed at temperature below 32 deg C. claim 1 ...

COMPOSITIONS AND METHODS COMPRISING THERMOLYSIN PROTEASE VARIANTS

The present invention provides serine protease—thermoslysine—variants produced there from. Specifically, the present invention provides serine protease variants having one or more substitutions as compared to a reference serine protease. In addition, the present invention provides compositions comprising these serine protease variants. In some embodiments, the present invention provides cleaning compositions comprising at least one of these serine protease variants. 12-. (canceled)3. A thermolysin enzyme variant or an active fragment thereof comprising an amino acid modification to a parent thermolysin enzyme , wherein the modification is a productive position , wherein the modifications tested at the productive position meet the following criteria: a position wherein the minimum performance indices (PI) relative to Thermolysin parent for at least three of the parameters of expression , detergent stability , thermostability , PAS-38 microswatch cleaning activity , or activity on Abz-AGLA-Nba are greater than or equal to 1 , andwherein the productive position is selected from the group consisting of (i) 278, 283, 180, 244, 48 and 63, or (ii) T278R, Q283E, A180E, I244T, T48E and F63C, wherein the amino acid positions of the thermolysin variant are numbered by correspondence with the amino acid sequence of thermolysin set forth in SEQ ID NO: 3.4. (canceled)5. A thermolysin enzyme variant or an active fragment thereof comprising an amino acid modification to a parent thermolysin enzyme , wherein the modification is at a productive position , wherein at least one modification of the modifications tested at the productive position meet the following criteria:a position wherein the minimum performance indices (PI) relative to Thermolysin parent for at least all of the parameters of expression, detergent stability, thermostability, PAS-38 microswatch cleaning activity, or activity on Abz-AGLA-Nba are greater than or equal to 0.5 and no more than one of the parameters is ...

USE AND PRODUCTION OF STORAGE-STABLE NEUTRAL METALLOPROTEASE

The present invention provides methods and compositions comprising at least one neutral metalloprotease enzyme that has improved storage stability. In some embodiments, the neutral metalloprotease finds use in cleaning and other applications. In some particularly preferred embodiments, the present invention provides methods and compositions comprising neutral metalloprotease(s) obtained from sp. In some more particularly preferred embodiments, the neutral metalloprotease is obtained from . In still further preferred embodiments, the neutral metalloprotease is a variant of the neutral metalloprotease. In yet additional embodiments, the neutral metalloprotease is a homolog of the the neutral metalloprotease. The present invention finds particular use in applications including, but not limited to cleaning, bleaching and disinfecting. 1Bacillus. An isolated neutral metalloprotease having improved storage stability , wherein said neutral metalloprotease is a neutral metalloprotease.2BacillusB. amyloliquefaciens.. The neutral metalloprotease of claim 1 , wherein said is3. The neutral metalloprotease of claim 1 , wherein said neutral metalloprotease has at least 45% amino acid identity with the neutral metalloprotease comprising SEQ ID NO:3.4. The neutral metalloprotease of claim 1 , wherein said neutral metalloprotease comprises the amino acid sequence set forth in SEQ ID NO:3.5. A nucleotide sequence encoding at least a portion of the neutral metalloprotease of claim 1 , wherein said nucleotide sequence is selected from of SEQ ID NOS:1 claim 1 , 2 claim 1 , 12 claim 1 , and 13.6. An expression vector comprising a nucleotide sequence encoding the amino acid sequence set forth in SEQ ID NO:3.7. A host cell comprising the expression vector of .8. A storage-stable neutral metalloprotease obtained from said host cell of claim 7 , wherein said neutral metalloprotease is encoded by said expression vector.9. An isolated neutral metalloprotease having immunological cross- ...

PROTEASES COMPRISING ONE OR MORE COMBINABLE MUTATIONS

The present invention provides engineered protease variants. In particular, the protease variants comprise combinable mutations at selected surface positions that affect the charge and/or hydrophobicity of the enzyme to enhance at least one desired property of the resulting variant enzyme in a chosen application. Compositions comprising the protease variants, and methods for using the same are also provided. 14-. (canceled)5BacillusBacillus. A cleaning composition comprising a subtilisin variant of a subtilisin , wherein said subtilisin variant is a mature form having proteolytic activity and comprising a substitution at two or more positions , wherein said subtilisin is GG36 , and wherein said substitution at two or more positions is selected from S24Q-R45Q-S101Q-G118Q-T213Q , R45Q-S101Q-G118Q-T213Q , S101Q-G118Q-T213Q , G118Q-T213Q , S24E-R45Q-S101Q-G118Q-T213Q , S24E-R45E-S101Q-G118Q-T213Q , S24E-R45E-S101E-G118Q-T213Q , S24E-R45E-S101E-Q109E-G118Q-T213Q , S24E-R45E-S101E-Q109E-G118E-T213Q , S24E-R45E-S101E-Q109E-G118E-T213E , S24L-R45Q-S101Q-G118Q-T213Q , S24L-R45L-S101Q-G118Q-T213Q , S24L-R45L-S101L-G118Q-T213Q , S24L-R45L-S101L-Q109L-G118Q-T213Q , S24L-R45L-S101L-Q109L-G118L-T213Q , S24L-R45L-S101L-Q109L-G118L-T213L , S24R-R45Q-S101Q-G118Q-T213Q , S24R-S101Q-G118Q-T213Q , S24R-S101R-G118Q-T213Q , S24R-S101R-Q109R-G118Q-T213Q , S24R-S101R-Q109R-G118R-T213Q , S24R-S101R-Q109R-G118R-T213R , S24E-S101R-Q109R-G118R-T213R , S24E-R45E-S101R-Q109R-G118R-T213R , S24E-R45E-S101E-Q109R-G118R-T213R , S24E-R45E-S101E-Q109E-G118R-T213R , S24E-R45E-S101E-Q109E-G118E-T213R , S24E-R45E-S101E-Q109E-G118E-T213E , S24Q-R45Q-S101Q-G118Q-T213Q-L217Q , and S24Q-R45Q-S101Q-G118Q-T213Q-L217E , wherein the positions correspond to the positions of BPN′ subtilisin of SEQ ID NO:1.6. (canceled)7BacillusBacillus. A cleaning composition comprising a subtilisin variant of a subtilisin , wherein said subtilisin variant is a mature form having proteolytic activity and comprising a substitution ...

LAUNDRY DETERGENT EFFECTIVE FOR USE AGAINST PET STAINS AND ODORS

A detergent is provided for removing pet odors and stains, the detergent including: one or more of a surfactant, a buffering agent, a preservative, an odor absorber, a builder, and an enzyme; and a fragrance that is non-toxic for pets. 1. A detergent for removing pet odors and stains , the detergent comprising: a surfactant,', 'a buffering agent,', 'a preservative,', 'an odor absorber,', 'a builder, and', 'an enzyme; and, 'one or more offrom about 0.1 to about 5 percent, by weight, of a fragrance that is non-toxic for pets.2. The detergent of claim 1 , the surfactant selected from the group consisting of but not limited to: C10-16 Alkylpolyglucoside claim 1 , lauramine oxide claim 1 , and decyl glucoside.3. The detergent of claim 1 , wherein the fragrance comprises an essential oil.4. The detergent of claim 3 , wherein the fragrance is selected from the group consisting of: chamomile claim 3 , lavender claim 3 , vanilla claim 3 , honey claim 3 , lemongrass.5. The detergent of claim 1 , the odor absorber selected from the group consisting of one or more of: zinc ricinoleate claim 1 , sodium lauroyl sarcosinate claim 1 , tetrahydroxypropyl ethylenediamine claim 1 , zinc chloride claim 1 , and beta-cyclodextrin.6. The detergent of claim 1 , the enzyme selected from the group consisting of one or more of: protease claim 1 , amylase claim 1 , alpha amylase claim 1 , mannanase claim 1 , pectate lyase claim 1 , lipase claim 1 , cellulase claim 1 , savinase claim 1 , ammonia monooxygenase claim 1 , and hydroxylamine oxidoreductase.7. The detergent of claim 1 , wherein the detergent is contained within a capsule.8. A detergent for removing pet odors and stains claim 1 , the detergent comprising:a surfactant selected from the group consisting of one or more of: C10-16 Alkylpolyglucoside, lauramine oxide, and decyl glucoside;a buffering agent selected from the group consisting of one or more of: glycerol oleate, sodium gluconate, sodium chloride, sodium citrate, sodium ...

DETERGENT COMPOSITIONS CONTAINING A BRANCHED SURFACTANT

The present invention relates generally to detergent compositions and, more specifically, to detergent compositions containing a branched surfactant. 2. A detergent composition according to wherein from about 0.5% to about 30% by weight of the first surfactant are isomers having m+n=10 claim 1 , from about 1% to about 45% by weight of the first surfactant are isomers having m+n=12 claim 1 , and from about 0.1% to about 20% by weight of the first surfactant are isomers having m+n=13.3. A detergent composition according to wherein from about 55% to about 75% by weight of the first surfactant are isomers having m+n=11 claim 1 , wherein from about 0.5% to about 30% by weight of the first surfactant are isomers having m+n=10; wherein from about 15% to about 45% by weight of the first surfactant are isomers having m+n=12 claim 1 , wherein from about 0.1% to about 20% by weight of the first surfactant are isomers having m+n=13 claim 1 , and wherein from about 0.001% to about 20% by weight of the first surfactant are surfactants of formula II.4. The detergent composition according to claim 1 , wherein at least about 25% by weight of the first surfactant are surfactants having m+n=10 claim 1 , m+n=11 claim 1 , m+n=12 claim 1 , and m+n=13 claim 1 , wherein n is 0 claim 1 , 1 claim 1 , or 2 claim 1 , or m is 0 claim 1 , 1 claim 1 , or 2.5. The detergent composition according to claim 1 , wherein X is selected from the group consisting of an ethoxylated sulfate claim 1 , a propoxylated sulfate claim 1 , a butoxylated sulfate claim 1 , and mixtures thereof.6. The detergent composition according to claim 1 , wherein X is an ethoxylated sulfate and the average degree of ethoxylation ranges from about 0.4 to about 5 claim 1 , or about 0.4 to about 3.5 claim 1 , or about 0.4 to about 1.5 claim 1 , or from about 0.6 to about 1.2 claim 1 , or about 2.5 to about 3.5.7. The detergent composition according to further comprising an adjunct cleaning additive selected from the group ...

Liquid Automatic Dish Washing Detergent Compositions

The stabilization of subtilisins by peptide aldehydes, hydrosulfite adducts thereof or peptide methyl ketones, is particularly effective in liquid ADW detergents which contain a strong sequestering builder. 1. A liquid dish wash detergent composition comprising:a) a strong sequestering builder,b) a subtilisin, andc) a subtilisin inhibitor which is a peptide aldehyde or a hydrosulfite adduct thereof or a peptide methyl ketone, wherein the methyl group is optionally halogen-substituted, and wherein the peptide optionally has an N-terminal protection group;wherein the composition is essentially devoid of an anionic surfactant.2. The composition of claim 1 , which has a content of non-ionic surfactant below 5% by weight.3. The composition of claim 1 , which comprises the strong sequestering builder in an amount above 0.1% by weight.4. The composition of claim 1 , wherein the strong sequestering builder is a phosphorus-containing builder.5. The composition claim 4 , which comprises the phosphorus-containing builder in an amount corresponding to a phosphorus content of at least 0.1% by weight of the composition claim 4 , particularly above 1% claim 4 , above 2% claim 4 , above 3% claim 4 , above 4% or above 5% by weight.6. The composition of claim 1 , which further comprises an additional detergent enzyme; preferably an amylase.7. The composition of claim 1 , wherein the inhibitor is an aldehyde or ketone having the formula P-(A)-L-(B)—B—R* or a hydrosulfite adduct of such aldehyde claim 1 , wherein:{'sub': 3', '3', '2', '2, 'a) R* is H (hydrogen), CH, CX, CHX, or CHX;'}b) X is a halogen atom;{'sup': '0', 'c) Bis a single amino acid residue with L- or D-configuration of the formula —NH—CH(R)—C(═O)—;'}d) x is 1, 2 or 3;{'sub': 'x', 'sup': '0', 'e) Bis independently a single amino acid residue, each connected to the next B or to Bvia its C-terminal;'}f) L is absent or independently a linker group of the formula —C(═O)—, —C(═O)—C(═O)—, —C(═S)—, —C(═S)—C(═S)— or —C(═S)—C(═O ...

DETERGENT COMPOSITIONS CONTAINING A STABILIZED ENZYME BY PHOSPHONATES

Detergent compositions that contain an enzyme, alkaline source, and phosphonate or amine phosphonate salt are described here. A use solution of the detergent compositions containing disclosed phosphonates can retain its enzyme activity for an extended period of time. Specifically, one specific type of phosphonates and another specific type of amine phosphonate salts were discovered to stabilize enzymes in detergent compositions. Solid detergent compositions that contain disclosed phosphonate or amine phosphonate salts are more effective to remove soils and can save production and use costs. 2. The solid detergent composition of claim 1 , wherein the solid detergent is produced by a cast claim 1 , extruded claim 1 , or press process.3. The solid detergent composition of claim 1 , wherein the solid detergent is a block claim 1 , tablet claim 1 , or particulate.4. The solid composition of claim 1 , wherein the solid detergent is a multi-use solid detergent.5. The solid detergent composition of claim 1 , wherein Ris —CH—PO(OH)group.6. The solid detergent composition of claim 1 , wherein Ris —CH—PO(OH)group and Ris ethanolyl claim 1 , diglyco claim 1 , substituted alkyl claim 1 , isopropyl-2-(EO)-biphosphonateamine claim 1 , or methyl-phosphonate.8. The solid detergent composition of claim 1 , wherein the alkaline source comprises a metal carbonate and metal bicarbonate.9. The solid detergent composition of claim 8 , wherein the mole ratio of the metal carbonate and the metal bicarbonate is from about 0.25:1 to about 1:0.25.10. The solid detergent composition of claim 1 , wherein the enzyme comprises a protease claim 1 , amylase claim 1 , lipase claim 1 , or mixture thereof.11. The solid detergent composition of claim 1 , further comprising an amine or salt thereof.12. The solid detergent composition of claim 11 , wherein the amine is fully neutralized.13. The solid detergent composition of claim 11 , wherein the amine comprises an alkanolamine claim 11 , ...