КОМПОЗИЦИИ МОЮЩИХ СРЕДСТВ

Изобретение относится к биотехнологии. Описана композиция моющего средства, содержащая бактериальный щелочной фермент, проявляющий эндо-бета-1,4-глюканазную активность, и этоксилированный сополимер, представляющий собой: 1) статистически привитый сополимер, имеющий гидрофильную основную цепь и гидрофобные боковые цепи, 2) модифицированный полиэтилениминовый сополимер, 3) модифицированный полиаминоамид, 4) негидрофобно модифицированный акриловый/полиэфирный гребнеобразноразветвленный сополимер, 5) их смеси, и вспомогательные материалы. Предложен способ очистки и/или обработки поверхности или ткани, включающий стадии введения в контакт поверхности или ткани с описанной композицией и необязательную стирку и/или полоскание поверхности или ткани. Изобретение позволяет расширить арсенал моющих средств. 2 н. и 21 з.п. ф-лы, 5 табл.

НОВАЯ ПРОТЕАЗА ГРИБОВ И ЕЕ ПРИМЕНЕНИЕ

Изобретение относится в области биотехнологии. Описан фермент сериновая протеаза грибов, имеющая аминокислотную последовательность зрелого фермента, которая по меньшей мере на 86% идентична аминокислотной последовательности зрелого фермента Fe_RF6318, представленной в описании. Раскрыты: выделенная нуклеиновая кислота, кодирующая указанный фермент; рекомбинантный вектор экспрессии, содержащий указанную нуклеиновую кислоту, функционально связанную с регуляторными последовательностями; и клетка-хозяин для получения фермента сериновой протеазы по настоящему изобретению, содержащая указанный рекомбинантный экспрессионный вектор. Предложен способ получения фермента или ферментного препарата, содержащего указанный фермент сериновой протеазы, при этом способ включает этап культивирования клетки-хозяина по настоящему изобретению и либо этап восстановления протеазы из клетки, либо этап выделения клетки из культуральной среды и получения супернатанта, содержащего протеазу. Описан ферментный препарат ...

СОСТАВ ДЛЯ ОЧИСТКИ ТВЕРДЫХ ПОВЕРХНОСТЕЙ С КОМПОНЕНТОМ ДЛЯ КОНТРОЛЯ НЕПРИЯТНОГО ЗАПАХА И СПОСОБЫ ОЧИСТКИ ТВЕРДЫХ ПОВЕРХНОСТЕЙ

Изобретение относится к составам для очистки твердых поверхностей, содержащим кислотный компонент; одно или более поверхностно-активных веществ; полимер, модифицирующий поверхность; компонент для контроля неприятного запаха, содержащий эффективное количество двух или более летучих альдегидов, выбранных из 2-этоксибензилальдегида, 2-изопропил-5-метил-2-гексеналя, 5-метилфурфураля, 5-метил-тиофен-карбоксальдегида, адоксаля, п-анисового альдегида, бензилальдегида, бургеналя, коричного альдегида, цималя, децилового альдегида, флораля супер, флоргидраля, гелионаля, лаурилового альдегида, лигустраля, лираля, мелоналя, о-анисового альдегида, пиноацетальдегида, Р.Т. буциналя, тиофенкарбоксальдегида, транс-4-деценаля, транс транс 2,4-нонадиеналя, ундецилового альдегида; и водный носитель, при этом компонент для контроля неприятного запаха содержит от 35% до 60% летучих альдегидов, имеющих В.Р. 250ºC или более и ClogP 3,0 или более; или 25% альдегидов, имеющих В.Р. приблизительно 250ºC или менее ...

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.

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.

ПРОТЕАЗА Streptomyces

Изобретение относится к биотехнологии и представляет собой новую сериновую протеазу, содержащую аминокислотную последовательность, которая по меньшей мере на 90% идентична последовательности протеазы 1AG3 Streptomyces дикого типа. Также настоящее изобретение относится к последовательностям нуклеиновых кислот, кодирующих протеазу, а также к клеткам-хозяевам, моющим композициям и корму для животных, содержащим предлагаемую сериновую протеазу. Изобретение позволяет расширить ассортимент ферментов, а именно сериновых протеаз, имеющих высокую ферментативную активность. 9 н. и 23 з.п. ф-лы, 8 ил., 16 табл., 13 пр.

РАСТВОРИМЫЕ ИЗДЕЛИЯ ЕДИНИЧНОЙ ДОЗЫ, СОДЕРЖАЩИЕ КАТИОННЫЙ ПОЛИМЕР

Изобретение относится к стабильным растворимым изделиям единичной дозы. Описано изделие для ухода за тканью, содержащее неводную жидкую композицию, содержащую катионный полимер - катионную целлюлозу, жирную кислоту или соль, воду и анионное поверхностно-активное вещество, при этом катионный полимер присутствует в форме частиц. Кроме этого, описан способ получения изделия единичной дозы. Технический результат - обеспечение изделия для ухода за тканью без ухудшения растворимости пленки и полезного эффекта при уходе за тканями. 2 н. и 7 з.п. ф-лы, 3 табл., 7 пр.

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 ...

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.

СОСТАВ, СОДЕРЖАЩИЙ МИКРОКАПСУЛЫ

Настоящее изобретение относится к жидкому моющему составу. Описан моющий состав, содержащий от 0,01 до 20 % по массе воды, микрокапсулы, содержащие полезный агент, и ионное соединение, имеющее, по меньшей мере, 2 анионных участка, при этом ионная сила, обеспечиваемая ионным соединением, имеющим, по меньшей мере, 2 анионных участка, превышает 0,045 моль/кг, при этом состав заключен в оболочку из водорастворимой пленки, микрокапсула содержит сердцевину и материал стенок, где материал стенок содержит смолу, включающую продукт реакции альдегида и амина, а полезный агент выбран из группы различных веществ. Технический результат - уменьшение утечки активного агента из микрокапсул, стабильность моющих составов. 10 з.п. ф-лы, 5 пр.

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.

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 ...

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, ...

КОМПОЗИЦИЯ ДЛЯ ОЧИСТКИ С ИСПОЛЬЗОВАНИЕМ СМЯГЧЕННОЙ ВОДЫ

... 1. Состав для очисти моющей системой, содержащей: от примерно 15% до примерно 75% по меньшей мере одного поверхностно-активного вещества; от примерно 0,01% до примерно 10% по меньшей мере одного фермента; менее чем примерно 1% моющего компонента, и менее чем примерно 1% хелата. 2. Состав по п.1, при этом моющая система содержит: зону мытья, способную вмещать субстрат; зону смягчения воды, жидкостно соединенную с зоной мытья, при этом вышеупомянутая зона мытья способна получать подаваемую воду и образовывать по меньшей мере частично смягченную воду. 3. Состав по п.1, при этом состав комбинируется с по меньшей мере частично смягченной водой, имеющей удельную электропроводность менее чем примерно 200 μСм/см. 4. Состав по п.2, при этом зона смягчения воды содержит нанофильтрацию, электродеионизацию, электродиализ, обратный осмос, дистилляцию, емкостную деионизацию и их комбинации. 5. Состав по п.4, при этом зона емкостной деионизации содержит по меньшей мере один электрод, содержащий активированный ...

ВАРИАНТЫ АЛЬФА-АМИЛАЗЫ С ПОВЫШЕННЫМИ УРОВНЯМИ ПРОДУКЦИИ В ПРОЦЕССАХ ФЕРМЕНТАЦИИ

... 1. Вариант первой α-амилазы дикого типа, где ! (a) вариант α-амилазы содержит по меньшей мере одну модифицированную аминокислоту по сравнению с первой α-амилазой дикого типа; ! (b) вариант α-амилазы обладает активностью α-амилазы; и ! (c) по меньшей мере одна модифицированная аминокислота является такой же, как аминокислота, обнаруженная в соответствующем положении аминокислотной последовательности второй α-амилазы, ! где вторая α-амилаза обладает большей растворимостью, чем первая α-амилаза дикого типа, в ферментационном бульоне, и ! где аминокислотная последовательность варианта α-амилазы отличается по меньшей мере одной аминокислотой от второй α-амилазы. ! 2. Вариант α-амилазы по п.1, где вариант α-амилазы, кроме того, можно экспрессировать на более высоком уровне в клетке-хозяине по сравнению с уровнем экспрессии первой α-амилазы дикого типа. ! 3. Вариант α-амилазы по п.1, где вариант α-амилазы содержит 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 20, 25, 30, 35 или 40 модификаций ...

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 ...

ФЕРМЕНТ ДЛЯ ПРОДУКЦИИ ДЛИНОЦЕПОЧЕЧНОЙ ПЕРКИСЛОТЫ

... 1. Выделенный пергидролазный фермент, который пергидролизует длинноцепочечные ацильные эфирные субстраты. ! 2. Выделенный пергидролазный фермент по п.1, который вызывает продукцию длинноцепочечной перкислоты в присутствии длинноцепочечного ацильного эфирного субстрата и перекиси. ! 3. Выделенный пергидролазный фермент по п.1, где указанный длинноцепочечный ацильный эфирный субстрат содержит цепь из по крайней мере шести атомов углерода. ! 4. Выделенный пергидролазный фермент по п.1, где указанный длинноцепочечный ацильный эфирный субстрат содержит цепь из по крайней мере девяти атомов углерода. ! 5. Выделенный пергидролазный фермент по п.1, аминокислотная последовательность которого идентична на по крайней мере 80% аминокислотной последовательности встречающегося в природе фермента пергидролазы. ! 6. Выделенный пергидролазный фермент по п.1, аминокислотная последовательность которого идентична на по крайней мере 80% аминокислотной последовательности пергидролазы дикого типа M. smegmatis ...

КОМПОЗИЦИИ, СОДЕРЖАЩИЕ ВАРИАНТЫ СЕРИНОВЫХ ПРОТЕАЗ, И СПОСОБЫ

... 1. Выделенный вариант субтилизина, где указанный вариант субтилизина представляет собой зрелую форму, имеющую протеолитическую активность и содержащую замены в трех или более положений, выбранных из: 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, 49, 50, 51, 52, 53, 54, 55, 56, 57, 58, 59, 60, 61, 62, 63, 64, 65, 66, 67, 68, 69, 71, 72, 73, 74, 75, 76, 77, 78, 79, 80, 81, 82, 83, 84, 85, 86, 87, 88, 89, 90, 91, 92, 93, 94, 95, 96, 97, 98, 99, 100, 101, 102, 103, 104, 105, 106, 107, 108, 109, 110, 111, 112, 113, 114, 115, 116, 117, 118, 119, 120, 121, 122, 123, 124, 125, 126, 127, 128, 129, 130, 131, 132, 133, 134, 135, 136, 137, 138, 139, 140, 141, 142, 143, 144, 145, 146, 147, 148, 149, 150, 151, 152, 153, 154, 155, 156, 157, 158, 159, 160, 161, 162, 163, 164, 165, 166, 167, 169, 170, 171, 172, 173, 174, 175, 176, 177, 178, 179, 180, 181, 182, 183, 184 ...

ВАРИАНТЫ СУБТИЛАЗ И КОДИРУЮЩИЕ ИХ ПОЛИНУКЛЕОТИДЫ

ЭЛЕКТРОЛИТИЧЕСКАЯ СИСТЕМА ДЛЯ АВТОМАТИЧЕСКОГО МЫТЬЯ ПОСУДЫ

СТИРКА С ДВУМЯ ЗАМАЧИВАНИЯМИ

... 1. Способ очистки объекта, включающий стадии:a. распределения по объекту первого раствора для замачивания, содержащего по меньшей мере одно поверхностно-активное вещество и по меньшей мере один фермент, за которым следует первый период замачивания, где концентрации по меньшей мере одного поверхностно-активного вещества и по меньшей мере одного фермента выше относительно их концентраций в последующем растворе для стирки;b. добавления к объекту второго раствора для замачивания, содержащего по меньшей мере один компонент, который отличается от любого из компонентов, содержащихся в растворе замачивания (a), с последующим вторым периодом замачивания;c. кроме того, добавления к объекту воды для получения раствора для стирки с последующим периодом стирки; иd. полоскания объекта;где стадию (b) проводят или до, или после стадии (c), и где указанный способ имеет эффективность стирки, соответствующую любому показателю из (i) относительной эффективности стирки (RWP) по меньшей мере 1; (ii) связанному ...

СОСТАВ, СОДЕРЖАЩИЙ МИКРОКАПСУЛЫ

... 1. Жидкий моющий состав, содержащий от приблизительно 0,01 до приблизительно 40% по массе воды, микрокапсулы, содержащие полезный агент, и ионное соединение, имеющее, по меньшей мере, 2 анионных участка, при этом ионное соединение обеспечивает ионную силу более, чем приблизительно 0,045 моль/кг.2. Жидкий моющий состав по п.1, отличающийся тем, что состав содержит от приблизительно 1 до приблизительно 25% по массе воды.3. Жидкий моющий состав по п.1, отличающийся тем, что полезный агент выбран из группы, состоящей из сырья отдушки, силиконовых масел, восков, углеводородов, высших жирных кислот, эфирных масел, липидов, охлаждающих кожу агентов, витаминов, солнцезащитных средств, антиоксидантов, глицерина, катализаторов, отбеливающих частиц, частиц диоксида кремния, агентов, уменьшающих неприятный запах, красителей, осветлителей, антибактериальных активных веществ, антиперспирантных активных веществ, катионных полимеров и их смесей.4. Жидкий моющий состав по п.1, отличающийся тем, что полезный ...

МОЮЩЕЕ И ЧИСТЯЩЕЕ СРЕДСТВО, СОДЕРЖАЩЕЕ КОМБИНАЦИЮ АМИЛАЗЫ И ПРОТЕАЗЫ

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 ...

ЖИДКОЕ МОЮЩЕЕ СРЕДСТВО

ВАРИАНТЫ АЛЬФА-АМИЛАЗ

ПРИМЕНЕНИЕ ВАРИАНТОВ ПРОТЕАЗЫ

... 1. Применение варианта субтилизина для мытья твердых поверхностей, где вариант содержит замены 9R, 15T, 68A, 245R и 218 {D,G,V} по сравнению с исходным субтилизином, и где положения соответствуют положениям зрелого полипептида SEQ ID NO:2 [BPN'].2. Применение по п.1, где в положении 218 осуществляют замену на D.3. Применение по п.1, где вариант дополнительно содержит по меньшей мере одну из следующих модификаций: G61{D,E}, N62{D,E}, N76{D,E}; *97aG, A98{G,S}, S99G, S101G, H120{N,V,Q,D}, P131{T,S}, Q137H, A194P, A228V, A230V, N261D.4. Применение по п.1, где вариант содержит следующие замены: S9R, A15T, V68A, N218D и Q245R.5. Применение по п.4, где вариант дополнительно содержит замену G61E.6. Применение по п.4, где вариант дополнительно содержит замену A98S.7. Применение по п.4, где вариант дополнительно содержит замену S99G.8. Применение по любому из пп.1-7, где вариант содержит следующие замены: S9R, A15T, G61E, V68A, A98S, S99G, N218D и Q245R.9. Применение по любому из пп.1-7, где исходный ...

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.

Neuartige Lipasevarianten zur Verwendung in Reinigungsmitteln

THERMOSTABILE PROTEASE AUS THERMOBACTEROIDES

ALKALISCHE PROTEASE UND VERFAHREN ZU IHRER HERSTELLUNG

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.

MUTANTEN DER alpha-AMYLASE

ENZYME UND WASCHMITTELZUSAMMENSETZUNGEN AUF ENZYMBASIS

MEHRFACH SUBSTITUIERTE PROTEASEVARIANTEN

WASCHEMITTELZUSAMMENSETZUNGEN MIT PROTEASEN UND VERBESSERTEN AMYLASEN

Enzymstabilisatoren

Die vorliegende Erfindung betrifft Wasch- oder Reinigungsmittel enthaltend mindestens eine Protease und mindestens eine Verbindung der Formel (I), (II), (III), IV), (V), (VI), (VII), (VIII), (IX), (X) oder (XI), wie hierin offenbart, die als Proteaseinhibitorwirkt und somit ein geeigneter Enzymstabilisator ist, sowie die Verwendung dieser Verbindungen als Enzymstabilisator in protease-haltigen Wasch- und Reinigungsmitteln. Ebenfalls Bestandteil der Erfindung sind die entsprechenden Wasch- und Reinigungsverfahren und die Verwendung der hierin beschriebenen Mittel.

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.

METHODEN ZUR VORBEHANDLUNG VON SCHUHEN

VERNETZTE, NICHT VON PILZEN KOMMENDE LIPASE ENTHALTENDE ZUSAMMENSETZUNG UND METHODEN ZU DEREN VERWENDUNG

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.

Fabric treatment article and method of use

Urinal cleaning routine

Fabric treatment article and corresponding method of using it

A process for reducing deterioration of colours of textile fabrics during washing

... 276,337. Henkel et Cie Ges. Aug. 17, 1926, [Convention date]. Cleansing-compositions; soaps. - In order to prevent the running of colours of textiles and for protecting their hue in washing, urea is added to the washing liquid, which may contain soap, tryptic enzymes, oxygen-evolving detergents, soda, waterglass, &c. The urea. may be added directly or as a solution or mixture with neutral or detergent agents or with water softeners. Specifications 276,338 and 276,339 are referred to.

DETERGENT COMPOSITIONS

Laundry detergent composition

A detergent composition, for removing in cold wash water oily soil from fibrous substrates includes: synthetic organic nonionic detergent, cationic surface active agent, and an amount, less than half of the detergents, of a water soluble C21 dicarboxylic salt, e.g., an ammonium salt. There may also be present an enzyme and/or a water soluble ionizable salt, which may be an inorganic builder for the detergent.

Method for textile laundering

The present invention comprises apparatus and process for laundering textiles based upon utilizing quantities of an aqueous liquid wash liquor in the wash step ranging from, at least, just enough to be substantially evenly and completely distributed onto all portions of the textiles to, at most, about 5 times the dry weight of the textiles to be laundered. This results in an extremely efficient use of the detergent composition. The present invention also comprises novel wash liquor and detergent compositions for use in said apparatus and process.

Detergent compositions

Detergent compositions

MACHINE DISHWASHING COMPOSITIONS

Detergent compositions containing amylase

A detergent composition comprising at least 1% of a surfactant characterised in that said detergent composition comprises the combination of a nonionic polysaccharide ether having a molecular weight of more than 10000 with an amylase enzyme selected from bacterial amylase, fungal amylase or mixtures thereof such that said detergent composition has an activity of at least O.OOIKNU (Kilo Novo Units) per gram or at least 0.01FAU (Fungal Alpha Amylase Units) per gram. A suitable polysaccharide ether is methyl cellulose.

BLEACHING AND CLEANING COMPOSITION

Automatic dishwashing detergent composition

Lignocellulose conversion processes and products

Detergent tablet

Liquid detergent

A liquid detergent comprising a component (A) which is a nonionic surfactant, a component (B) which is an anionic surfactant, a component (C) which is a protease, a component (D) which is a water-soluble polymer having at least one unit selected from the group consisting of an alkylene terephthalate unit and an alkylene isophthalate unit and at least one unit selected from the group consisting of an oxyalkylene unit and a polyoxyalkylene unit, and a component (E) which is at least one component selected from the group consisting of an α-hydroxy-monocarboxylic acid and a salt thereof, wherein the sum total of the contents of all of the surfactants is 45 mass% or more relative to the total mass of the liquid detergent and the content of the component (B) is 4 mass% or more relative to the total mass of the liquid detergent.

Coated bleach particle

New dishwashing machine and method

Composition

A liquid laundry detergent composition comprises (a) from 20 percent to 40 percent by weight of the composition of a surfactant system, wherein the surfactant system comprises a first nonionic surfactant (A), a second nonionic surfactant (B), and anionic surfactants; (b) from 0.1 wt% to 20wt% polyhydric C2-CB alcohol; (c) a bleaching agent or enzymatic system; d) a pH regulating agent wherein the composition has a neat pH of from 2 to 7; and wherein the composition has a viscosity of above 200000 cps, measured at 1 s"1 at 20 degrees centigrade. Also shown is a method of manufacture and use of the composition.

Enzyme activity enhancement

PROTEOLYTIC ENZYME AND ITS PREPARATION

... 1330390 Dough improvers RHONE-POULENC SA 29 Oct 1971 [30 Oct 1970] 50384/71 Heading A2B [Also in Divisions C3 and C5] Foodstuffs contain the proteolytic enzyme 25, 048 RP produced by aerobically cultivating Streptomyces nebuloxes DS 14, 579 NRRL 3864. Specific examples refer to a bread dough comprising wheat flour, yeast, salt, water and enzyme 25, 048 RP and a concentrate used in biscuit making comprising starch and enzyme 25, 048 RP. The presence of the enzyme in the bread dough facilitates working the dough, reduces the fermentation time, and provides a more uniform cell structure in the loaf.

Novel proteins for the treatment of cellulosic material

2,6-BETA-D-FRUKTANHYDROLASE ENZYME AND PROCEDURE FOR ITS USE

PROCEDURE FOR THE MARK TREATMENT

LIQUID DETERGENT WITH BLEACH ADDITIVE

AMYLOLYTI ENZYMES WITH IMPROVED CHARACTERISTICS, DERIVED FROM the ALPHA AMYLASE FROM B. LICHENIFORMIS

MULTIPLESUBSTITUTED PROTEASEVARIANTEN

SUBTILASEVARIANTEN WITH CHANGE IMMUNOGENITÄT

DETERGENT COMPOSITIONS

SMELL PROCEDURE AND PRODUCT

PROCEDURE FOR THE STAIN REMOVAL OF CLOTHES CARRIED BY AT THE BODY

MUTANTEN THE ALPHA AMYLASE

WASCH- UND REINIGUNGSMITTELMISCHUNG

SUBTILASEN

NEW LIPASEVARIANTEN FOR USE IN CLEANING AGENTS

MODIFIED POLYPEPTID

FOAM-PRODUCING KIT CONTAINING A FOAM DONOR AND A COMPOSITION WITH HIGH ONE TENSIDANTEIL

PROCEDURE FOR MACHINE CLEANING OF TEXTILES OR CELEBRATIONS ARTICLES

FOAM ARMS DETERGENTS

SUBTILASE ENZYMES OF THE I-S1 AND I-S2 SUB-GROUPS WITH AT LEAST AN ADDITIONAL AMINO ACID BETWEEN POSITION 97 AND 98

ALKALINE AMYLASE OUT BACILLUS

SUBSTITUTED SEVERAL TIMES PROTEASEVARIANTEN WITH CHANGED NET LOAD FOR THE USE IN DETERGENTIEN

PROTEASE WITH IMPROVED STABILITY IN DETERGENTIEN

POLYPEPTIDE WITH ALKALINER ALPHA AMYLASE ACTIVITY AND FOR THESE CODING NUCLEIC ACIDS

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.

Novel Variant Hypocrea Jecorina CBH2 Cellulases

Described herein are variants of H. jecorina CBH2, a Cel6A enzyme. The present invention provides novel cellobiohydrolases that have altered thermostability.

Granule With Reduced Dust Potential

A granule with an allergenic component has reduced dust by including antifoam added during the production of the granule. The antifoam may be dispersed throughout the granule or added to one of the components of the granule. The granule with antifoam produces at least 30% less dust than a comparable granule produced according to a process in which no antifoam is added.

Polymer-containing cleaning compositions and methods of production and use thereof

The present invention provides detergent compositions, essentially free of peroxygen or chlorine bleach compounds, containing one or more surfactants, one or more builders, one or more enzymes and one or more low MW (e.g., 0.8-25 kDa) polyethyleneimine (PEI) polymers or salts thereof, and methods of producing such compositions. The compositions of the invention provide certain benefits in cleaning of textiles (particularly fabrics including clothing), hard surfaces and dishware and utensils, including enhanced removal of certain difficult-to-remove stains such as chocolate pudding and grass, as well as of polyphenolic stains such as cherry juice, blueberry juice, red wine, tea and coffee. The invention also provides methods of using these compositions in laundry, hard surface cleaning and dishwashing applications.

Halomonas Strain WDG195-Related Alpha-Amylases, And Methods Of Use, Thereof

Compositions and methods relating to an alpha-amylase enzyme obtained from Halomonas variabilis WDG195 are described.

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.

Machine dishwasher detergent

Cleaning agent combinations comprising a cleaning agent preparation B further comprising: (b1) at least one non-ionic surfactant; and (b2) at least one active cleaning enzyme; and a rinsing composition C further comprising: (c1) at least one non-ionic surfactant, are by virtue of their thermal stability particularly suitable for automatic dosing in automatic dishwashing. The cleaning agent combinations of the present invention also have the characterizing feature of markedly improved cleaning performance in comparison to conventional methods.

Alpha-amylase variant 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 properties relative to the parent alpha-amylase.

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.

Stabilization Of Perhydrolases

Disclosed herein are enzyme powders comprising a spray-dried formulation of at least one CE-7 esterase, at least one oligosaccharide excipient, and optionally at least one surfactant. Also disclosed herein is a process for producing peroxycarboxylic acids from carboxylic acid esters using the aforementioned enzyme powders. Further, disinfectant and laundry care formulations comprising the peracids produced by the processes described herein are provided.

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.

Cleaning compositions comprising amylase variants reference to a sequence listing

The present invention relates to cleaning compositions comprising variants of an alpha-amylase and methods of treating surfaces such as textiles with aqueous liquor comprising such compositions, especially at low temperatures.

Process For Preparing An Enzyme Containing Granule

This invention relates to a process for manufacture of a dry enzyme containing mixer granulation granule comprising the step of adding a particulate component to the mixer granulation process, wherein the particulate component constitutes less than 75 parts of the finished granule and the particles of the particulate component have an mean size of more than 40 μm in its longest dimension. Also claimed is granules of the process, granules containing more than two particles of the particulate component and composition and methods of using the granules.

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 ...

MACHINE DISHWASHER DETERGENT

A liquid cleaning agent containing: a) 20 to 70 wt % water, b) at least one amylase preparation, c) at least one Ca-ion source, d) lactic acid or a lactic acid salt, is notable for elevated amylase stability and improved cleaning performance. 1. A liquid cleaning agent containing:a) 20 to 70 wt % water;b) at least one amylase preparation;{'sup': '2+', 'c) at least one Ca-ion source;'}d) lactic acid or a lactic acid salt.2. The liquid cleaning agent according to claim 1 , wherein the weight proportion of the active protein of the amylase preparation in terms of the total weight of the cleaning agent is between 0.001 and 5.0 wt %.3. The liquid cleaning agent according to claim 1 , wherein the liquid cleaning agent contains calcium lactate claim 1 , and wherein the weight proportion of the calcium lactate in terms of the total weight of the cleaning agent is from 0.05 to 10 wt %.5. The liquid cleaning agent according to claim 1 , wherein the cleaning agent contains at least one alditol claim 1 , and wherein the weight proportion of the alditol in terms of the total weight of the cleaning agent is from 1.0 to 10 wt %.6. The liquid cleaning agent according to claim 1 , wherein the cleaning agent contains at least one nonionic surfactant claim 1 , and wherein the weight proportion of the nonionic surfactant in terms of the total weight of the cleaning agent is from 0.5 to 10 wt %.7. The liquid cleaning agent according to claim 1 , wherein the cleaning agent contains at least one complexing agent from the group of the phosphonates claim 1 , and wherein the weight proportion of the phosphonate in terms of the total weight of the cleaning agent is from 0.1 to 8.0 wt %.8. The liquid cleaning agent according to claim 1 , wherein the cleaning agent contains at least one hydrophobically modified polymer claim 1 , and wherein the weight proportion of the hydrophobically modified polymer in terms of the total weight of the cleaning agent is from 0.1 to 10 wt %.9. A method for ...

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 ...

Phosphate And Phosphonate-Free Automatic Gel Dishwashing Detergent Providing Improved Spotting and Filming Performance

A phosphate and phosphonate-free gel automatic dishwashing detergent provides improved spotting and filming performance by including a spot reduction system that contains a combination of a polyacrylate and a carboxymethyl inulin. The gel detergent may also be free of a bleach ingredient (i.e., it does not contain either chlorine bleach or an oxygen bleach).

Perhydrolase variant providing improved specific activity

An acetyl xylan esterase variant having perhydrolytic activity is provided for producing peroxycarboxylic acids from carboxylic acid esters and a source of peroxygen. More specifically, a Thermotoga maritima acetyl xylan esterase gene was modified using error-prone PCR and site-directed mutagenesis to create an enzyme catalyst characterized by an increase in specific activity. The variant acetyl xylan esterase may be used to produce peroxycarboxylic acids suitable for use in a variety of applications such as cleaning, disinfecting, sanitizing, bleaching, wood pulp processing, and paper pulp processing applications.

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.

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 ...

Methods and materials for reducing biofilms

This document provides methods and materials related to reducing biofilms. For example, enzymes (e.g., glycosyl hydrolases), nucleic acid molecules encoding enzymes, host cells containing nucleic acid encoding enzymes, and methods for using enzymes to reduce biofilms and infections associated with biofilms are provided.

STABILIZED LIQUID TENSIDE PREPARATION COMPRISING ENZYMES

A hydrolytic enzyme is to be stabilized in a liquid surfactant preparation. This is achieved by using a component that stabilizes the hydrolytic enzyme and encompasses a multiply substituted benzenecarboxylic acid that has a carboxyl group on at least two carbon atoms of the benzene residue. 1. A liquid surfactant preparation comprising a hydrolytic enzyme and a component stabilizing the hydrolytic enzyme , wherein the component stabilizing the hydrolytic enzyme comprises a multiply substituted benzenecarboxylic acid that has a carboxyl group on at least two carbon atoms of the benzene residue.2. The surfactant preparation according to claim 1 , wherein the multiply substituted benzenecarboxylic acid is a benzenecarboxylic acid having four carboxyl groups on the benzene residue.3. The surfactant preparation according to claim 1 , wherein the multiply substituted benzenecarboxylic acid is pyromellitic acid.4. The surfactant preparation according to claim 1 , wherein the multiply substituted benzenecarboxylic acid is contained in a quantity from 0.000001 to 10 wt %; and the hydrolytic enzyme is contained in a quantity from 1×10to 5 weight percent claim 1 , based on active protein.5. The surfactant preparation according to claim 1 , wherein the hydrolytic enzyme is a protease claim 1 , amylase claim 1 , cellulase claim 1 , glycosidase claim 1 , hemicellulase claim 1 , mannanase claim 1 , xylanase claim 1 , xyloglucanase claim 1 , xanthanase claim 1 , pectinase claim 1 , β-glucosidase claim 1 , carrageenase claim 1 , lipase claim 1 , or mixtures thereof.6. The surfactant preparation according to claim 1 , wherein the surfactant preparation further comprises at least one additional ingredient selected from the group consisting of builder claim 1 , nonaqueous solvent claim 1 , acid claim 1 , water-soluble salt claim 1 , thickening agent claim 1 , disinfecting ingredient claim 1 , and combinations thereof.7. A washing or cleaning method claim 1 , in which a hydrolytic ...

STABILIZED LIQUID TENSIDE PREPARATION COMPRISING ENZYMES

A hydrolytic enzyme is stabilized in a liquid surfactant preparation using a component that stabilizes the hydrolytic enzyme and encompasses an oligoaminobiphenyl oligocarboxylic acid. 1. A liquid surfactant preparation encompassing a hydrolytic enzyme and a component stabilizing the hydrolytic enzyme , wherein the component stabilizing the hydrolytic enzyme comprises an oligoaminobiphenyl oligocarboxylic acid.2. The surfactant preparation according to claim 1 , wherein the oligoaminobiphenyl oligocarboxylic acid is a diaminobiphenyl dicarboxylic acid.3. The surfactant preparation according to claim 1 , wherein the oligoaminobiphenyl oligocarboxylic acid is 3 claim 1 ,3-diamino-[1 claim 1 ,1-biphenyl]-2 claim 1 ,4-dicarboxylic acid.4. The surfactant preparation according to claim 1 , wherein the oligoaminobiphenyl oligocarboxylic acid is contained in a quantity from 0.000001 to 10 wt %; and the hydrolytic enzyme is included in a quantity from 1×10to 5 weight percent claim 1 , based on active protein.5. The surfactant preparation according to claim 1 , wherein the hydrolytic enzyme is selected from the group consisting of a protease claim 1 , amylase claim 1 , cellulase claim 1 , glycosidase claim 1 , hemicellulase claim 1 , mannanase claim 1 , xylanase claim 1 , xyloglucanase claim 1 , xanthanase claim 1 , pectinase claim 1 , β-glucosidase claim 1 , carrageenase claim 1 , and a lipase claim 1 , or is a mixture that encompasses at least two of said enzymes.6. The surfactant preparation according to claim 1 , wherein the preparation is a washing agent claim 1 , cleaning agent claim 1 , or disinfection agent.7. The surfactant preparation according to claim 1 , wherein the surfactant preparation moreover comprises at least one further ingredient that is selected from the group consisting of builder claim 1 , nonaqueous solvent claim 1 , acid claim 1 , water-soluble salt claim 1 , thickening agent claim 1 , disinfecting ingredient claim 1 , and combinations thereof.8. A ...

STABILIZED LIQUID TENSIDE PREPARATION COMPRISING ENZYMES

A hydrolytic enzyme is stabilized in a liquid surfactant preparation using a component that stabilizes the hydrolytic enzyme and includes a phenylalkyldicarboxylic acid. 1. A liquid surfactant preparation encompassing a hydrolytic enzyme and a component stabilizing the hydrolytic enzyme , wherein the component stabilizing the hydrolytic enzyme encompasses a phenylalkyldicarboxylic acid.2. The surfactant preparation according to claim 1 , wherein the phenylalkyldicarboxylic acid is phenylmalonic acid.3. The surfactant preparation according to claim 1 , wherein the phenylalkyldicarboxylic acid is contained in a quantity from 0.000001 to 10 wt %; and/or the hydrolytic enzyme is contained in a quantity from 1×10to 5 weight percent claim 1 , based on active protein.4. The surfactant preparation according to claim 1 , wherein the hydrolytic enzyme is selected from the group consisting of a protease claim 1 , amylase claim 1 , cellulase claim 1 , glycosidase claim 1 , hemicellulase claim 1 , mannanase claim 1 , xylanase claim 1 , xyloglucanase claim 1 , xanthanase claim 1 , pectinase claim 1 , β-glucosidase claim 1 , carrageenase claim 1 , and a lipase claim 1 , or is a mixture that encompasses at least two of said enzymes.5. The surfactant preparation according to claim 1 , wherein the surfactant preparation is a washing agent claim 1 , cleaning agent claim 1 , or disinfection agent.6. The surfactant preparation according to claim 1 , wherein the surfactant preparation further comprises at least one further ingredient that is selected from the group consisting of builder claim 1 , nonaqueous solvent claim 1 , acid claim 1 , water-soluble salt claim 1 , thickening agent claim 1 , disinfecting ingredient claim 1 , and combinations thereof.7. A method claim 1 , in particular a washing or cleaning method claim 1 , comprising:stabilizing a hydrolytic enzyme in a wash bath using a component that comprises a phenylalkyldicarboxylic acid, the enzyme being selected from the group ...

Stabilized liquid tenside preparation comprising enzymes

A hydrolytic enzyme is to be stabilized in a liquid surfactant preparation. This is achieved by using a component that stabilizes the hydrolytic enzyme and encompasses an aminophthalic acid.

STABILIZED LIQUID TENSIDE PREPARATION COMPRISING ENZYMES

A hydrolytic enzyme is to be stabilized in a liquid surfactant preparation. This is achieved by using a component that stabilizes the hydrolytic enzyme and encompasses a phthaloylglutamic acid and/or a phthaloylaspartic acid. 1. A liquid surfactant preparation encompassing a hydrolytic enzyme and a component stabilizing the hydrolytic enzyme , wherein the component stabilizing the hydrolytic enzyme comprises a phthaloylglutamic acid.2. The surfactant preparation according to claim 1 , wherein the phthaloylglutamic acid is contained in a quantity from 0.000001 to 10 wt % claim 1 , and the hydrolytic enzyme is contained in a quantity from 1×10to 5 weight percent claim 1 , based on active protein.3. The surfactant preparation according to claim 1 , wherein the hydrolytic enzyme is selected from the group comprising a protease claim 1 , amylase claim 1 , cellulase claim 1 , glycosidase claim 1 , hemicellulase claim 1 , mannanase claim 1 , xylanase claim 1 , xyloglucanase claim 1 , xanthanase claim 1 , pectinase claim 1 , β-glucosidase claim 1 , carrageenase claim 1 , lipase claim 1 , and a mixture that encompasses at least two of said enzymes.4. The surfactant preparation according to claim 1 , wherein the preparation is a washing agent claim 1 , cleaning agent claim 1 , or disinfection agent.5. The surfactant preparation according to claim 1 , wherein the surfactant preparation moreover comprises at least one further ingredient that is selected from the group consisting of builder claim 1 , nonaqueous solvent claim 1 , acid claim 1 , water-soluble salt claim 1 , thickening agent claim 1 , disinfecting ingredient claim 1 , and combinations thereof.6. A washing or cleaning method claim 1 , comprising:stabilizing a hydrolytic enzyme in a washing using a component that stabilizes the hydrolytic enzyme and comprises a phthaloylglutamic acid, wherein the enzyme is selected from the group consisting of protease, amylase, cellulase, glycosidase, hemicellulase, mannanase, ...

STABILIZED LIQUID ENZYME-CONTAINING SURFACTANT PREPARATION

A hydrolytic enzyme is stabilized in a liquid surfactant preparation by using a component that stabilizes the hydrolytic enzyme and includes a monosaccharide glycerate. 1. A liquid surfactant preparation encompassing a hydrolytic enzyme and a component stabilizing the hydrolytic enzyme , wherein the component stabilizing the hydrolytic enzyme comprises a monosaccharide glycerate.2. The surfactant preparation according to claim 1 , wherein the monosaccharide glycerate is included in a quantity from 0.000001 to 10 wt %; and/or the hydrolytic enzyme is included in a quantity from 1×10to 5 weight percent claim 1 , based on active protein.3. The surfactant preparation according to claim 1 , wherein the monosaccharide glycerate is selected from the group consisting of an aldose glycerate claim 1 , a semiacetal of an aldose glycerate claim 1 , a ketose glycerate claim 1 , and a semiketal of a ketose glycerate.4. The surfactant preparation according to claim 1 , wherein the monosaccharide in the monosaccharide glycerate is selected from the group consisting of a triose residue claim 1 , a tetrose residue claim 1 , a pentose residue claim 1 , and a hexose residue.5. The surfactant preparation according to claim 4 , wherein the monosaccharide is the triose residue and is selected from the group consisting of glycerol aldehyde and dihydroxyacetone.6. The surfactant preparation according to claim 4 , wherein the monosaccharide is the tetrose residue and is selected from the group consisting of erythrose claim 4 , threose claim 4 , and erythrulose.7. The surfactant preparation according to claim 4 , wherein the monosaccharide is the pentose residue and is selected from the group consisting of ribose claim 4 , arabinose claim 4 , xylose claim 4 , lyxose claim 4 , deoxyribose claim 4 , ribulose claim 4 , and xylulose.8. The surfactant preparation according to claim 4 , wherein the monosaccharide is the hexose residue and is selected from the group consisting of altrose claim 4 , ...

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.

LIQUID DETERGENT COMPOSITION

A liquid detergent composition containing (A) 10 to 70 mass % of a nonionic surfactant, (B) 1 to 15 mass % of an anionic surfactant, (C) 0.01 to 2 mass % of a protease, and (D) 0.001 to 0.1 mass % of at least one compound selected from the group consisting of thiazole-based compounds and sulfur-containing amino acids. 1. A liquid detergent composition comprising: (A) 10 to 70 mass % of a nonionic surfactant , (B) 1 to 15 mass % of an anionic surfactant , (C) 0.01 to 2 mass % of a protease , and (D) 0.001 to 0.1 mass % of at least one compound selected from the group consisting of thiazole-based compounds and sulfur-containing amino acids.2. The liquid detergent composition according to claim 1 , further comprising (E) a calcium salt.3. The liquid detergent composition according to claim 1 , further comprising (G) an α-hydroxy-monocarboxylic acid or a salt thereof.4. The liquid detergent composition according to claim 3 , wherein the component (G) is at least one compound selected from the group consisting of lactic acid and sodium lactate.5. The liquid detergent composition according to claim 1 , further comprising (F) at least one enzyme selected from the group consisting of cellulases and lipases. The present invention relates to a liquid detergent composition.Priority is claimed on Japanese Patent Application No. 2010-202886, filed Sep. 10, 2010, the content of which is incorporated herein by reference.Detergent compositions used in laundering textile items such as clothing or fabrics typically contain a surfactant as a detergent component. Further, a variety of other additives are also added for the purpose of imparting various functions, including detergent builders such as alkaline agents, enzymes, hydrotropic agents, preservatives, antibacterial agents, fluorescent brightening agents, colorants, fragrances and antioxidants.Among the various additives added to detergent compositions, enzymes are an important functional material, and are used as an additive ...

ENZYME FABRIC CARE TABLETS FOR CONSUMERS AND METHODS

Single-dose enzyme tablets for direct sale to consumers are provided for boosting the performance of automatic laundry and dish washing operations using conventional detergents. The tablets provide a wash performance that is better than or at least equal to the wash performance of the detergents alone even when the time and or temperature of the wash cycle is decreased. The tablets may be provided in kits and the enzymes are selected to treat a variety of fabric stains as well as to provide fabric care benefits. 1. A method for providing enzymes to consumers for boosting the wash performance of a conventional laundry or dish detergent in a laundry or dish washer; the method comprising: selecting at least one enzyme for laundry or dish detergent applications; combining the at least one enzyme with at least binders or fillers; manufacturing tablets from the combined enzyme and binders or fillers; and packaging the tablets for sale to consumers with instructions for use. This application is a divisional of U.S. application Ser. No. 11/988,467, filed Dec. 21, 2009, which is the National Stage of International Application No. PCT/US2006/026705, filed Jul. 11, 2006, which claims the benefit of U.S. Provisional Application No. 60/698,386, filed Jul. 11, 2005, which are hereby incorporated by reference in their entirety.This invention relates to enzymes for direct sale to consumers. More specifically, the invention relates to enzyme tablets for use by consumers, the tablets enhancing and/or supplementing the performance of commercially available fabric and dish care products and providing a cleaning benefit. Yet more specifically, the invention relates to a variety of enzyme tablets with different enzymes and enzyme combinations for selection by a consumer to provide enhanced cleaning, and/or to provide stain specific cleaning, and/or to provide fabric enhancements, and/or to provide a cleaning benefit when added by the consumer to cleaning and fabric care procedures using ...

COMPOSITIONS AND METHODS FOR SURFACE TREATMENT WITH LIPASES

Methods and compositions for treating textiles and hard surfaces with compositions having specific lipases are described. The compositions have increased stability to oxidative degradation in particular due to bleach catalysts. 3. A method of manufacturing a detergent composition comprising a lipase exhibiting improved stability to oxidative degradation , comprising the step of mixing a lipase variant with a detergent adjunct , wherein the lipase variant has improved stability to oxidative degradation compared to the mature polypeptide of SEQ ID NO:1 and wherein the variant has lipase activity.4. A method according to wherein the lipase variant comprises a substitution at one or more of the positions selected from the group of positions corresponding to T37 claim 3 , N39 and G91 of the mature polypeptide of SEQ ID NO:1.6. A method according to wherein the lipase is mixed with a bleach component.7. A method according to wherein the bleach component comprises a bleach catalyst that is capable of accepting an oxygen atom from a peroxyacid and transferring the oxygen atom to an oxidizeable substrate and (ii) a diacyl and/or tetraacyl peroxide species.8. A method according to wherein the bleach catalyst comprises an oxazidinium and/or dioxirane functional group claim 1 , and/or is capable of forming an oxaziridinium and/or a dioxirane functional group upon acceptance of an oxygen atom.11. A method according to wherein Ris selected from the group consisting of 2-butyloctyl claim 10 , 2-pentylnonyl claim 10 , 2-hexyldecyl claim 10 , iso-tridecyl and iso-pentadecyl.12. A method according to wherein the parent lipase comprises an amino acid sequence with at least 60% identity with the mature polypeptide of SEQ ID NO: 1; consists of the amino acid sequence of the mature polypeptide of SEQ ID NO: 1 claim 1 , or a fragment thereof having lipase activity.13. A method according to wherein the variant is:a. a polypeptide comprising an amino acid sequence with at least 60% identity ...

FABRIC TREATMENT COMPOSITIONS COMPRISING TARGET BENEFIT AGENTS

The invention provides a composition comprising: a) a benefit agent (preferably perfume) delivery particle comprising a poly-xyloglucan or poly-galactomannan with a ratio of beta-1,4 to 1,6 linkages of 1:1 to 3:1, or a mixture thereof as a delivery aid, b) a mannanase, preferably in combination with one or more of lipase, protease and amylase. Preferably the delivery particle is a core-shell encapsulate. 1. A composition comprising:a) a benefit agent delivery particle comprising a poly-xyloglucan or poly-galactomannan with a ratio of beta-1,4 to 1,6 linkages of 1:1 to 3:1, or a mixture thereof as a delivery aid,b) a mannanase.2. A composition according to wherein the benefit agent delivery particle comprises a further polymer.3. A composition according to any preceding claim wherein the benefit agent delivery particle comprises a perfume.4. A composition according to any preceding claim wherein the benefit agent delivery particle comprises a core and one or more shells surrounding said core.5. A composition according to any preceding claim which further comprises one or more of lipase claim 1 , protease and amylase.6. A composition according to which comprises each of lipase claim 5 , protease and amylase.7. A composition according to any preceding claim wherein the benefit agent delivery particle is a core/shell particle with perfume present in the core and an aminoplast shell claim 5 , the shell be surrounded with a outer layer of polyvinyl acetate claim 5 , said outer layer also comprising a poly-xyloglucan delivery aid. The present invention relates to fabric treatment compositions and, more specifically, to compositions comprising particles which comprise a benefit agent (preferentially perfume) and the deposition aid. The invention also relates to delivery of the benefit agent (preferably perfume) to fabric during laundering.The present invention will be described with particular reference to perfume although the technology is believed applicable to other ...

DETERGENT COMPOSITION

An automatic dishwashing detergent composition comprising by weight of the composition: 1. An automatic dishwashing detergent composition comprising by weight of the composition:a) at least 9% of coated bleach particles the particles having a coating comprising at least 5% by weight of the particle of an efflorescent material;b) at least 0.5% of granulates containing active enzyme wherein the granulates comprise at least 30% of efflorescent material by weight of the granulate and wherein the efflorescent material and the active enzyme are in a weight ratio of at least 4:1.2. An automatic dishwashing detergent composition comprising by weight of the composition:a) at least 9% of coated bleach particles the particles having a coating comprising at least 5% by weight of the particle of an efflorescent material;b) at least 0.5% of granulates containing active enzyme wherein the granulates comprise at least 50% of efflorescent material.3. A composition according to further comprising from 0.1 to 5% of an ethoxylated/propoxylated non ionic surfactant by weight of the composition.4. A composition according to wherein the automatic dishwashing detergent composition is in unit dose form.5. A composition according to wherein the weight of the composition is less than about 20 grams.6. A composition according to wherein the bleach is an inorganic peroxide.7. A composition according to wherein the efflorescent material is selected from the group consisting of sodium citrate claim 1 , sodium sulphate and mixtures thereof.8. A composition according to wherein the composition is free of phosphate and comprises a non-phosphate detergent builder.9. A composition according to wherein the composition comprises an anti-scaling polymer.11. A composition according to further comprising from 0.1 to 5% of an ethoxylated/propoxylated non ionic surfactant by weight of the composition.12. A composition according to wherein the automatic dishwashing detergent composition is in unit dose form ...

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.

PROTEIN-ENHANCED SURFACTANTS FOR ENZYME ACTIVATION

Disclosed herein are compositions containing enzymes, particularly acting at the interface between two immiscible phases where the rate of enzymatic activity is increased by addition of a blend of surfactant(s) and a mixture derived from yeast fermentation, that contain non-enzymatic exo-proteins released by yeast in response to a non-lethal stress. The enzymes include those that work at the interface between an aqueous solution and a water immiscible phase, liquid or solid, such as oil, fat, cellulose, lignin, etc. including, but not limited to the following or combinations thereof: lipases, polysaccharase, lignase, cellulase and the like, in which the substrate of an enzymatic reaction forms a phase, segregated from the aqueous solution in which the enzymes are typically operating. Disclosed herein are methods for improving a washing solution with the use of these compositions, where the enzyme-protein-surfactant solution can be used in such applications as: laundry, spot remover, pre-laundry, dishes, hard surface cleaning, wastewater treatment, cellulose breakdown as in ethanol production, lignin utilization, environmental remediation, industrial cleaning, and agricultural applications. 1. A composition comprising non-enzymatic exo-proteins , a surfactant and an enzyme.2. The composition of claim 1 , wherein the exo-proteins are derived from yeast fermentation process.3Saccharomyces cerevisiae.. The composition of claim 2 , wherein the yeast is4. The composition of claim 2 , wherein the fermentation process is aerobic.5. The composition of claim 2 , wherein the fermenting yeast is subject to a stress condition.6. The composition of claim 5 , wherein the stress is a non-lethal heat shock.7. The composition of claim 1 , wherein the enzyme is selected from the group claim 1 , or combinations thereof: lipase claim 1 , cellulase claim 1 , lignase claim 1 , polysaccharase.8. The composition of claim 1 , wherein the surfactant is anionic claim 1 , nonionic claim 1 , ...

STABILIZED, LIQUID, ENZYME-CONTAINING SURFACTANT PREPARATION

The aim of the invention is to stabilize a hydrolytic enzyme in a liquid surfactant preparation. Said aim is achieved by using a component stabilizing the hydrolytic enzyme, said component comprising boric acid, propylene glycol and a phenylboronic acid derivative having the structural formula (I) in which R is hydrogen, a hydroxyl group, a C1-C6 alkyl group, a substituted C1-C6 alkyl group, a C1-C6 alkenyl group or a substituted C1-C6 alkenyl group. 2. The surfactant preparation according to claim 1 , wherein the residue R in the phenylboronic acid derivative is a C-Calkyl group or hydrogen.3. The surfactant preparation according to claim 1 , wherein the phenylboronic acid derivative is 4-formylphenylboronic acid.4. The surfactant preparation according to claim 1 , comprising 0.05 to 5.5 wt. % boric acid claim 1 , 0.000001 to 10 wt. % propylene glycol claim 1 , 0.001 to 0.08 wt. % phenylboronic acid derivative claim 1 , and 1×10to 5 wt. % hydrolytic enzyme claim 1 , based on active protein.5. The surfactant preparation according to claim 1 , wherein the hydrolytic enzyme is selected from a group of enzymes consisting of protease claim 1 , amylase claim 1 , cellulase claim 1 , glycosidase claim 1 , hemicellulase claim 1 , mannanase claim 1 , xylanase claim 1 , xyloglucanase claim 1 , xanthanase claim 1 , pectinase claim 1 , β-glucosidase claim 1 , carrageenase or a lipase or a combination comprising at least two of the enzymes from the group.6. The surfactant preparation according to claim 1 , wherein the surfactant preparation further comprises at least one additional ingredient selected from the group consisting of builder claim 1 , non-aqueous solvent claim 1 , acid claim 1 , water-soluble salt claim 1 , thickener claim 1 , disinfecting ingredient and combinations thereof. The present invention generally relates to liquid, enzyme-containing surfactant preparations as used, for example, in washing, cleaning or disinfecting, and more particularly relates to such a ...

Liquid surfactant preparation containing lipase and phosphonate

A liquid surfactant preparation comprises a phosphonate and has an advantageous lipolytic activity. This is achieved by using a lipase that is naturally present in a microorganism, the microorganism being Rhizopus oryzae or Mucor javanicus.

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

According to the invention, storage stability in terms of cellulolytic activity is to be improved in a liquid washing or cleaning agent which comprises a protease and cellulase. 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(al) 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) a cellulase.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),(i) combinations of the amino acids ( ...

Enhanced oil recovery compositions comprising proteins and surfactants and methods of using the same

Disclosed herein are methods of using compositions as enhanced oil recovery agents, cleaning agents or as agents that improve the function of surfactants, the compositions comprising a surfactant and a protein system, where the protein system comprises proteins and stress proteins obtained by the process of fermenting yeast to obtain a fermentation mixture; subjecting the fermentation mixture to stress conditions to obtain a post-fermentation mixture; and centrifuging the post-fermentation mixture and obtaining the supernatant; where the protein mixture retains its functionality under extreme conditions.

UNIT-DOSE FORMAT PERHYDROLASE SYSTEMS

Described are compositions and methods relating to unit-dose format perhydrolase enzyme systems for use in cleaning applications, such as laundry and dishwashing. 1. A unit-dose package for delivering a perhydrolase enzyme system in a cleaning application , the perhydrolase enzyme system comprising a perhydrolase enzyme component , an acyl substrate component , and a peroxide source component , the package comprising:a first compartment at least partially bounded by a water-soluble material and comprising a first component of the perhydrolase enzyme system;a second compartment at least partially bounded by a water-soluble material and comprising a second component and a third component of the perhydrolase enzyme system;wherein the first component in the first compartment and the second and third components in the second compartment are separated during storage to prevent the formation of peracids, and wherein upon dissolution in an aqueous solution the first compartment and second compartment dissolve simultaneously or sequentially to permit contact of the first, second, and third components of the perhydrolase enzyme system to generate peracid.2. The unit-dose package of claim 1 , wherein the first component is the perhydrolase enzyme claim 1 , the second component is the acyl substrate claim 1 , and the third component is the peroxide source.3. The unit-dose package of claim 1 , wherein the first component is the acyl substrate claim 1 , the second component is the perhydrolase enzyme claim 1 , and the third component is the peroxide source.4. The unit-dose package of claim 1 , wherein the first component is the peroxide source claim 1 , the second component is the acyl substrate claim 1 , and the third component is the perhydrolase enzyme.5. The unit-dose package of claim 1 , wherein a very low-water claim 1 , non-aqueous claim 1 , or non-mixing form of laundry or dishwashing detergent is additionally provided in the first compartment.6. The unit-dose package of ...

ENZYME STABILIZED DETERGENT COMPOSITIONS

Biodegradable detergent compositions comprising enzymes and 1,3-propanediol are provided. The 1,3-propanediol in the composition is biologically derived and enhances the stability of the enzymes in the composition. The compositions also exhibit a low anthropogenic COemission profile. 1. A detergent composition comprising 1 ,3-propanediol and an enzyme , wherein the composition is biodegradable and wherein the 1 ,3-propanediol is biologically derived and enhances the stability of the enzyme.2. The composition of claim 1 , wherein the weight percent of enzyme in the composition is between about 0.0001% and about 5.0%.3. The composition of claim 1 , wherein the enzyme is selected from the group consisting of amylase claim 1 , protease claim 1 , Alcalase® claim 1 , and Termamyl®.4. The composition of claim 1 , further comprising borate or boric acid.5. The composition of claim 4 , wherein the weight percent of borate or boric acid in the composition is less than about 5.0%.6. The composition of claim 1 , wherein the composition is substantially free of borate or boric acid.7. The composition of claim 1 , wherein the 1 claim 1 ,3-propanediol has 50% biobased carbon.8. The composition of claim 1 , wherein the 1 claim 1 ,3-propanediol has 100% biobased carbon.9. The composition of claim 1 , wherein said detergent composition is selected from the group consisting of dish-washing detergents claim 1 , laundry detergents claim 1 , clothing softeners claim 1 , laundry bar soaps and car wash detergents.10. The composition of claim 1 , wherein the composition has a lower anthropogenic COemission profile as compared to a biodegradable composition comprising 1 claim 1 ,3-propanediol with a bio-based carbon content of 0%.11. A method of enhancing enzyme stability in a detergent composition containing an enzyme claim 1 , the method comprising the step of providing a detergent composition containing an enzyme claim 1 , and combining 1 claim 1 ,3-propanediol to the detergent ...

Pectate Lyase Variants

The present invention relates to pectate lyase variants exhibiting alterations relative to a parent enzyme exhibiting pectate lyase activity as its major enzymatic activity; to a method of producing such enzymes; and to methods for using such enzymes in the textile, detergent and cellulose fiber processing industries. Compared to the parent enzyme, the pectate lyase variants of the present invention exhibit improved stability in detergents.

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 ...

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 ...

Detergent Compositions Comprising Metalloproteases

The present invention relates to cleaning and/or detergent compositions comprising metalloproteases (E.C 3.4.24). The invention further concerns the use of the metalloproteases in cleaning processes, such as dish wash and laundry, and in particular to the use in low temperature wash and in removal of egg stains. Further the invention concerns methods of doing cleaning, such as dish wash and laundry. 112-. (canceled)13. A method for cleaning comprising contacting a surface in need of cleaning with a metalloprotease at a temperature of 40° C. or below14. The method of claim 13 , wherein the temperature is 35° C. or below.15. The method of claim 13 , wherein the temperature is 30° C. or below.16. The method of claim 13 , wherein the cleaning process is a laundry process.17. The method of claim 13 , wherein the cleaning process is a dish wash process.18. The method of claim 13 , wherein the metalloprotease is a Thermolysin-Like Metalloprotease comprising an active cleft motif: TG[TS][QS]DNGGVH[TI].19. The method of claim 13 , wherein the metalloprotease is a Thermolysin-Like Metalloprotease comprising an active cleft motif: DPDHYSKRYTG[TS][QS]DNGGVH[TI]NSGI.20. The method of claim 13 , wherein the metalloprotease is a Thermolysin-Like Metalloprotease comprising an active cleft motif: NT[TS][QS]DNGGVH[TI]NSGI.21. The method of claim 13 , wherein the metalloprotease is a Thermolysin-Like Metalloprotease selected from the group consisting of:a) an M4 metalloprotease of the MEROPS subclass M04.001;b) an M4 metalloprotease of the MEROPS subclass M04.018; andc) an M4 metalloprotease of the MEROPS subclass M04.021.22. The method of claim 13 , wherein the metalloprotease is an M7 Metalloprotease.23. The method of claim 13 , wherein the metalloprotease is an M35 Metalloprotease.24. The method of claim 13 , wherein the metalloprotease comprises an amino acid sequence having at least 80% sequence identity to the mature polypeptide of SEQ ID NOs: 1 claim 13 , 2 claim 13 , 3 claim ...

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+ ...

COMPOSITIONS

A composition comprising: (a) a lipolytic enzyme; (b) a hydrophobin, as defined herein; and optionally (c) a detergent; is provided. The composition is useful as a cleaning composition for removing lipid-based stains from surfaces. 1. A composition comprising:(a) a lipolytic enzyme; and {'br': None, 'sub': 1', 'n', '1', '1', 'a', '2', '2', 'b', '3', '3', 'c', '4', '4', 'd', '5', '5', 'e', '6', '6', 'f', '7', '7', 'g', '8', '2', 'm, '(Y)-B-(X)-B-(X)-B-(X)-B-(X)-B-(X)-B-(X)-B-(X)-B-(Y)\u2003\u2003(I)'}, '(b) a hydrophobin having the general formula (I) m and n are independently 0 to 2000;', {'sub': 1', '2', '3', '4', '5', '6', '7', '8', '1', '8, 'claim-text': [{'sub': 1', '2', '3', '4', '5', '6', '7', '1', '2, 'X, X, X, X, X, X, X, Yand Yindependently represent any amino acid;'}, 'a is 1 to 50;', 'b is 0 to 5;', 'c is 1 to 100;', 'd is 1 to 100;', 'e is 1 to 50;', 'f is 0 to 5; and', 'g is 1 to 100., 'B, B, B, B, B, B, Band Bare each independently amino acids selected from Cys, Leu, Ala, Pro, Ser, Thr, Met or Gly, at least 6 of the residues Bthrough Bbeing Cys;'}], 'wherein2. A composition according to claim 1 , wherein the lipolytic enzyme has triacylglycerol hydrolysing activity (E.C. 3.1.1.3).3. A composition according to claim 1 , wherein the lipolytic enzyme is a GX lipolytic enzyme claim 1 , wherein G is glycine and X is an oxyanion hole-forming amino acid residue claim 1 , wherein the GX lipolytic enzyme belongs to an alpha/beta hydrolase superfamily selected from the group consisting of abH23 claim 1 , abH25 claim 1 , and abH15.4. A detergent composition comprising the composition of .56-. (canceled)7. A composition according to claim 3 , wherein the GX lipolytic enzyme belongs to an alpha/beta hydrolase superfamily selected from the group consisting of abH23.01 claim 3 , abH 25.01 claim 3 , abH16.01 and abH15.02.8. A composition according to claim 3 , wherein the oxyanion hole forming residue X is selected from the group consisting of M claim 3 , Q claim 3 , ...

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.

Detergent Compositions Comprising Mettaloproteases

The present invention relates to the use of M7 or M35 Metalloproteases in cleaning processes, such as laundry and dish wash. The invention also relates to detergent compositions and cleaning compositions comprising M7 or M35 Metalloproteases. 115-. (canceled)16. A method of cleaning , said method comprising the steps of: contacting a surface in need of cleaning with an M7 or M35 Metalloprotease.17. The method of claim 16 , wherein the protease comprises an amino acid sequence having at least 70% sequence identity to the mature polypeptide of SEQ ID NOs: 1 claim 16 , 2 claim 16 , 3 claim 16 , 4 claim 16 , 5 or 6.18. The method of claim 16 , wherein the polypeptide comprises an amino acid sequence having at least 90% sequence identity to the mature polypeptide of SEQ ID NOs: 1 claim 16 , 2 claim 16 , 3 claim 16 , 4 claim 16 , 5 or 6.19. The method of claim 16 , wherein the cleaning process is a laundry process.20. The method of claim 16 , wherein the cleaning process is a dish wash process.21. The method of claim 16 , wherein the cleaning process is performed at a temperature of 40° C. or below.22. The method of claim 16 , wherein the cleaning process is performed at a pH between 5.5 and 9.23. A composition comprising a M7 or M35 Metalloprotease and a surfactant.24. The composition of claim 23 , wherein the protease comprises an amino acid sequence having at least 70% sequence identity to the mature polypeptide of SEQ ID NOs: 1 claim 23 , 2 claim 23 , 3 claim 23 , 4 claim 23 , 5 or 6.25. The composition of claim 23 , wherein the polypeptide comprises an amino acid sequence having at least 90% sequence identity to the mature polypeptide of SEQ ID NOs: 1 claim 23 , 2 claim 23 , 3 claim 23 , 4 claim 23 , 5 or 6.26. The composition of claim 23 , further comprising at least one additional enzyme selected from the group consisting of carbohydrases claim 23 , peptidases claim 23 , proteases claim 23 , lipases claim 23 , cellulase claim 23 , xylanases or cutinases or a ...

DETERGENTS OR CLEANING AGENTS HAVING A SOLID ENZYME FORMULATION

In a washing or cleaning agent that contains a solid enzyme formulation, the intention is to improve shelf stability in terms of enzymatic activity. This is achieved by a washing or cleaning agent comprising an enzyme granulate, the granulate comprising, besides the enzyme, the following components: (a) 68 to 90 wt % (w/w) sulfate, in particular alkali metal sulfate, particularly preferably sodium sulfate, (b) 0.1 to 10.5 wt % (w/w) polyethylene glycol, (c) 0.5 to 14.5 wt % (w/w) granulation adjuvant. 1. A washing or cleaning agent comprising an enzyme granulate , the granulate comprising , besides the enzyme , the following components:(a) 68 to 90 wt % (w/w) sulfate,(b) 0.1 to 10.5 wt % (w/w) polyethylene glycol,(c) 0.5 to 14.5 wt % (w/w) granulation adjuvant.2. The washing or cleaning agent according to claim 1 , characterized in that it contains the enzyme granulate in a quantity from 0.01 to 20 wt % (w/w).3. The washing or cleaning agent according to claim 1 , wherein component (c) is selected from the group consisting of cellulose claim 1 , sheet silicate claim 1 , carboxymethyl cellulose claim 1 , carboxymethyl starch claim 1 , methyl cellulose claim 1 , hydroxyethyl cellulose claim 1 , hydroxypropyl cellulose claim 1 , cellulose mixed ethers claim 1 , gelatin claim 1 , casein claim 1 , tragacanth claim 1 , maltodextrose claim 1 , sucrose claim 1 , invert sugar claim 1 , glucose syrup claim 1 , polyacrylate claim 1 , polymethacrylate claim 1 , copolymers of acrylic acid with maleic acid or vinyl-group-containing compounds claim 1 , polyvinyl alcohol claim 1 , partially saponified polyvinyl acetate claim 1 , and polyvinylpyrrolidone.4. The washing or cleaning agent according to claim 1 , wherein the enzyme is present in the enzyme granulate in a quantity from 2 to 30 wt % (w/w).5. The washing or cleaning agent according to claim 1 , wherein the enzyme granulate further comprises a color pigment in a quantity from 2 to 6 wt % (w/w).6. The washing or cleaning ...

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. 129-. (canceled)30. An isolated polypeptide having cellobiohydrolase I activity , which has at least 80% identity with the sequence of amino acids 1 to 452 of SEQ ID NO:16.31. The polypeptide of claim 30 , which has at least 85% identity with the sequence of amino acids 1 to 452 of SEQ ID NO:16.32. The polypeptide of claim 30 , which has at least 90% identity with the sequence of amino acids 1 to 452 of SEQ ID NO:16.33. The polypeptide of claim 30 , which has at least 95% identity with the sequence of amino acids 1 to 452 of SEQ ID NO:16.34. The polypeptide of claim 30 , which has at least 97% identity with the sequence of amino acids 1 to 452 of SEQ ID NO:16.35. The polypeptide of claim 30 , which has at least 98% identity with the sequence of amino acids 1 to 452 of SEQ ID NO:16.36. The polypeptide of claim 30 , which has at least 99% identity with the sequence of amino acids 1 to 452 of SEQ ID NO:16.37. The polypeptide of claim 30 , comprising the sequence of amino acids 1 to 452 of SEQ ID NO:16.38. The polypeptide of claim 30 , which is a fragment of the sequence of amino acids 1 to 452 of SEQ ID NO:16.39. 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. 13/681,490 filed on Nov. 20, 2012, now allowed, which is a divisional of U.S. application Ser. No ...

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. 129.-. (canceled)30. An isolated polypeptide having cellobiohydrolase I activity , which has at least 80% identity with the sequence of amino acids 1 to 525 of SEQ ID NO:60.31. The polypeptide of claim 30 , which has at least 85% identity with the sequence of amino acids 1 to 525 of SEQ ID NO:60.32. The polypeptide of claim 30 , which has at least 90% identity with the sequence of amino acids 1 to 525 of SEQ ID NO:60.33. The polypeptide of claim 30 , which has at least 95% identity with the sequence of amino acids 1 to 525 of SEQ ID NO:60.34. The polypeptide of claim 30 , which has at least 97% identity with the sequence of amino acids 1 to 525 of SEQ ID NO:60.35. The polypeptide of claim 30 , which has at least 98% identity with the sequence of amino acids 1 to 525 of SEQ ID NO:60.36. The polypeptide of claim 30 , which has at least 99% identity with the sequence of amino acids 1 to 525 of SEQ ID NO:60.37. The polypeptide of claim 30 , comprising the sequence of amino acids 1 to 525 of SEQ ID NO:60.38. The polypeptide of claim 30 , which is a fragment of the sequence of amino acids 1 to 525 of SEQ ID NO:60.39. 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. 13/681,490 filed on Nov. 20, 2012, now allowed, which is a divisional of U.S. application Ser. ...

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 ...

Variants of An Alpha-Amylase With Improved Production Levels in Fermentation Processes

Variants of Bacillus sp. no. 707 alpha-amylase are provided that are produced more efficiently and thus more economically. Higher fermentation yields are achieved through introducing amino acid variations that promote solubility of the variant in a fermentation broth. Increased solubility allows more enzyme to remain in solution after expression in a host cell. This in turn increases the efficiency with which the expressed variant enzyme can be recovered from the fermentation broth.

Targeted perhydrolases

Disclosed herein are compositions and methods to target enzymatic peracid production to a target surface. The peracid benefit agent produced by the targeted perhydrolytic enzyme can be use for a variety of applications such as bleaching, whitening, disinfecting, destaining, deodorizing, and combinations thereof. Specifically, a fusion protein comprising a perhydrolytic enzyme and at least one peptidic component having affinity for a target surface (excluding body surfaces and oral care surfaces) is used in combination with a suitable substrate and a source of peroxygen to enzymatically produce a peracid on or near the surface of the target material. In a preferred aspect, the target surface is a cellulosic material.

DETERGENT COMPOSITIONS CONTAINING BACILLUS AGARADHAERENS MANNANASE AND METHODS OF USE THEREOF

The present compositions and methods relate to an endo-β-mannanase cloned from , polynucleotides encoding the endo-β-mannanase, and methods of use thereof. Formulations containing the endo-β-mannanase are highly suitable for use as detergents. 1. A recombinant polypeptide comprising a catalytic domain of an endo-β-mannanase , wherein the catalytic domain is at least 90% identical to the amino acid sequence of SEQ ID NO:10 or a mature from of an endo-β-mannanase , wherein the mature form is at least 85% identical to the amino acid sequence of SEQ ID NO:7.2. (canceled)3. The recombinant polypeptide of claim 1 , wherein the polypeptide has mannanase activity in the presence of detergent.4. The recombinant polypeptide of claim 1 , wherein the polypeptide has mannanase activity in the presence of a protease.5. The recombinant polypeptide of claim 1 , wherein the polypeptide retains greater than 70% mannanase activity at pH values of between 5 and 6.6. The recombinant polypeptide of claim 1 , wherein the polypeptide retains greater than 70% mannanase activity at a temperature range from 40° C. to 55° C.7. The recombinant polypeptide of claim 1 , wherein the polypeptide is capable of hydrolyzing a substrate selected from the group consisting of chocolate ice cream claim 1 , guar gum claim 1 , locust bean gum claim 1 , and combinations thereof.8. The recombinant polypeptide of claim 1 , wherein the amino acid sequence is at least 95% identical to one of the group consisting of SEQ ID NOS:4-10.9. (canceled)10. The recombinant polypeptide of claim 1 , further comprising a native or non-native signal peptide.11. The recombinant polypeptide of claim 1 , wherein the polypeptide does not further comprise a carbohydrate-binding module.12. A detergent composition comprising the recombinant polypeptide of .13. The detergent composition of claim 12 , further comprising a surfactant.14. The detergent composition of claim 13 , wherein the surfactant is an ionic surfactant.15. The ...

Detergent compositions containing bacillus sp. mannanase and methods of use thereof

The present compositions and methods relate to an endo-B-mannanase cloned from a Bacillus sp., polynucleotides encoding the endo-B-mannanase, and methods of use thereof. Formulations containing the endo-β-mannanase are highly suitable for use as detergents.

Polypeptides Having Cellulolytic Enhancing Activity And Nucleic Acids Encoding Same

The present invention relates to isolated polypeptides having cellulolytic enhancing 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 for producing and using the polypeptides.

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 ...

STABLE ENZYME STABILIZER PREMIX

The need for a highly concentrated enzyme stabilizer premix, which is both physically and chemically stable, is met by dissolving phenyl boronic acid, or a derivative thereof, to form a premix comprising an organic solvent, while limiting the amount of water present. 1. A liquid premix comprising:at least about 5% by weight of an enzyme stabilizer selected from: phenyl boronic acid, derivatives of phenyl boronic acid, and mixtures thereof;and at least 10% by weight of organic solvent;wherein the premix comprises less than about 25% by weight of water.2. The premix according to claim 1 , wherein the premix comprises at least about 15% and no greater than about 65% by weight of the enzyme stabilizer.3. The premix according to claim 2 , wherein the premix comprises at least about 30% and no greater than about 51% by weight of the enzyme stabilizer.4. The premix according to claim 1 , wherein the premix comprises less than about 20% by weight of water.5. The premix according to claim 4 , wherein the premix comprises less than about 15% by weight of water.6. The premix according to claim 5 , wherein the premix comprises less than about 1% by weight of water.7. The premix according to claim 1 , wherein the premix comprises from about 10% to about 95% by weight of organic solvent.8. The premix according to claim 7 , wherein the premix comprises from about 24% to about 70% by weight of organic solvent.9. The premix according to claim 7 , wherein the organic solvent has Hansen Solubility parameters of:{'sub': 'p', 'sup': '0.5', '(a) delta polarity (δ) of from about 4 to about 22 MPa, and'}{'sub': 'h', 'sup': '0.5', '(b) delta H-bonding (δ) of from about 8 to about 32 MPa.'}10. The premix according to claim 9 , wherein the organic solvent has Hansen Solubility parameters of:{'sub': 'p', 'sup': '0.5', '(a) delta polarity (δ) of from about 8 to about 21 MPa, and'}{'sub': 'h', 'sup': '0.5', '(b) delta H-bonding (δ) of from about 11 to about 27 MPa.'}11. The premix according to ...

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 ...

Polypeptides Having N-Acetyl Glucosamine Oxidase Activity

The present invention relates to polypeptides having N-acetyl glucosamine oxidase 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. 115-. (canceled)16. A polypeptide having N-acetyl-D-glucosamine oxidase activity , selected from the group consisting of:(a) a polypeptide having at least 75% sequence identity to the mature polypeptide of SEQ ID NO: 2;(b) a polypeptide encoded by a polynucleotide that hybridizes under high stringency conditions with (i) the mature polypeptide coding sequence of SEQ ID NO: 1, (ii) the cDNA sequence thereof, or (iii) the full-length complement of (i) or (ii);(c) a polypeptide encoded by a polynucleotide having at least 75% sequence identity to the mature polypeptide coding sequence of SEQ ID NO: 1 or the cDNA sequence thereof; and(d) a fragment of the polypeptide of (a), (b), or (c) that has N-acetyl-D-glucosamine oxidase activity.17. The polypeptide of claim 16 , comprising or consisting of SEQ ID NO: 2 or the mature polypeptide of SEQ ID NO: 2.18. The polypeptide of claim 16 , wherein the mature polypeptide is amino acids 20 to 632 of SEQ ID NO: 2.19. The polypeptide of claim 16 , which has at least 20% of the antimicrobial activity of the mature polypeptide of SEQ ID NO: 2.20. The polypeptide of claim 19 , wherein the antimicrobial activity is assessed using a method described in Example 6 claim 19 , 7 claim 19 , 8 claim 19 , or 9.21Aspergillus carbonariusAspergillus niger. The polypeptide of claim 19 , wherein the antimicrobial activity is assessed as fungicidal or sporicidal effect towards any of the fungal strains BR00732 (CBS 139193) and strain BR00883 (accession number CBS 139194).22. A cleaning composition consisting of the polypeptide of and one or more ingredients used in cleaning compositions claim 16 , such as a surfactant.22. A method of cleaning and/ ...

POLYPEPTIDES HAVING RNASE ACTIVITY

The present invention relates to polypeptides having RNase 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 of the clades EYTV , EAD or YPH having RNase activity , selected from the group consisting of:(a) a polypeptide having at least 80% sequence identity to the polypeptide of SEQ ID NO: 3;(b) a polypeptide having at least 80% sequence identity to the polypeptide of SEQ ID NO: 6;(c) a polypeptide having at least 80% sequence identity to the polypeptide of SEQ ID NO: 9;(d) a polypeptide having at least 80% sequence identity to the polypeptide of SEQ ID NO: 12;(e) a polypeptide having at least 80% sequence identity to the polypeptide of SEQ ID NO: 15;(f) a polypeptide having at least 80% sequence identity to the polypeptide of SEQ ID NO: 57;(g) a polypeptide having at least 80% sequence identity to the polypeptide of SEQ ID NO: 58;(h) a polypeptide having at least 80% sequence identity to the polypeptide of SEQ ID NO: 59;(i) a polypeptide having at least 80% sequence identity to the polypeptide of SEQ ID NO: 60;(j) a polypeptide having at least 80% sequence identity to the polypeptide of SEQ ID NO: 61;(k) a polypeptide having at least 80% sequence identity to the polypeptide of SEQ ID NO: 62;(l) a polypeptide having at least 80% sequence identity to the polypeptide of SEQ ID NO: 63;(m) a polypeptide having at least 80% sequence identity to the polypeptide of SEQ ID NO: 64;(n) a polypeptide having at least 80% sequence identity to the polypeptide of SEQ ID NO: 65;(o) a polypeptide having at least 80% sequence identity to the polypeptide of SEQ ID NO: 66;(p) a polypeptide having at least 80% sequence identity to the polypeptide of SEQ ID NO: 67;(q) a polypeptide having at least 80% sequence identity to the polypeptide of SEQ ID NO: 72;(r) a polypeptide having at least 80% ...

Method for Mixing of Particles

Continuous mixing in a static mixer possible can be used to add one kind of particles (such as an enzyme granular product) in a small amount to a larger amount of a different kind of particles (such as a powder stream of detergent powder), even if the powder characteristics are substantially different, with substantially no damage to the enzyme particles and with a high degree of homogeneity. 1. A method for mixing of at least two kinds of particles , wherein a first and a second stream of particles are mixed in a static mixer , and wherein the first and the second stream of particles have a weight ratio below 1:20.2. The method of wherein the ratio is below 1:50 claim 1 , particularly in the range from 1:1000 to 1:100 claim 1 , or from 1:500 to 1:125.3. The method of claim 1 , wherein the average particle size of the first stream of particles is in the range 100-2000 μm.4. The method of claim 1 , wherein the average particle size of the first stream of particles is in the range 300-1200 μm.5. The method of claim 1 , wherein the coefficient of variation of the amount of particles from the first stream claim 1 , in the resulting mixture of the first and second stream of particles claim 1 , is less than 40%.6. The method of claim 5 , wherein the coefficient of variation is measured using at least 9 samples and a sample size of at least 5 g.7. The method of claim 1 , wherein the first stream comprises enzyme particles.8. The method of claim 7 , wherein the enzyme particles comprise a protease claim 7 , an amylase claim 7 , a carbohydrase claim 7 , a lipase claim 7 , a cellulase claim 7 , an oxidoreductase claim 7 , a mannanase or a pectate lyase or a phosphatase claim 7 , or a deoxyribonuclease.9. The method of claim 7 , wherein the resulting mixture of the enzyme particles and the second stream of particles has an amount of free enzyme dust below 20 parts per billion.10. The method of claim 1 , wherein the second stream comprises detergent granules or detergent powder ...

CHROMATOGRAPHY MEDIA AND ION EXCHANGE RESIN PERFORMANCE RESTORATION

An ion exchange resin rejuvenation system includes a vessel, a source of a first cleaning solution including an enzyme fluidly connected to the vessel, a source of a second cleaning solution fluidly connected to the vessel, a source of rinse solution connected to the vessel, and a source of a resin regeneration solution fluidly connected to the vessel. 113.-. (canceled)14. A method of rejuvenating ion exchange resin , the method comprising:treating an ion exchange resin contaminated with a protein layer with a first cleaning solution including an enzyme to provide a stripped ion exchange resin and protein fragments.15. The method of claim 14 , wherein treating the ion exchange resin with the first cleaning solution includes treating the ion exchange resin with a protease.16. The method of claim 15 , wherein treating the ion exchange resin with the first cleaning solution includes treating the ion exchange resin with subtilisin.17. The method of claim 14 , wherein treating the ion exchange resin with the first cleaning solution includes treating the ion exchange resin with the first cleaning solution at a temperature of about 55° C.18. The method of claim 14 , wherein treating the ion exchange resin with the first cleaning solution includes treating the ion exchange resin with the first cleaning solution at a pH of about 9.19. The method of claim 14 , further comprising backwashing the protein fragments.20. The method of claim 14 , further comprising treating the stripped ion exchange resin with a second cleaning solution to provide a cleaned ion exchange resin.21. The method of claim 20 , wherein treating the stripped ion exchange resin with the second cleaning solution comprises treating the stripped ion exchange resin with an acid.22. The method of claim 20 , wherein treating the stripped ion exchange resin with the second cleaning solution includes treating the stripped ion exchange resin with at least one of a caustic solution claim 20 , a base solution claim 20 ...

Detergent Composition

A detergent composition comprising a subtilisin variant having the amino acid sequence set forth in SEQ ID NO: 1, and at least one additional ingredient selected from i) bleaches selected from percarbonates, persulphates and organic peracids, ii) aminocarboxylates, or iii) sulphonated polymers, or iv) organophosphoric acids or salts thereof and mixtures thereof is provided. Also provided is a detergent composition comprising a subtilisin variant having the amino acid sequence set forth in SEQ ID NO: 1, wherein the detergent composition is at least partially enveloped in a water soluble or water dispersible package. The compositions exhibit good performance on proteinaceous stains, even when formulated at alkaline pHs. A method of removing proteinaceous stains from surfaces comprising such stains is also provided. 1. A method of automatic dishwashing , comprising supplying a detergent composition to an automatic dishwasher machine , wherein the detergent composition comprises: bleaches selected from percarbonates, persulphates and organic peracids,', 'aminocarboxylates, or', 'sulphonated polymers, or', 'organophosphonic acids or salts thereof, and mixtures thereof., 'a subtilisin variant having the amino acid sequence set forth in SEQ ID NO: 1, and at least one additional ingredient selected from2. The method according to claim 1 , wherein the subtilisin variant having the amino acid sequence set forth in SEQ ID NO: 1 is an isolated variant.3. The method according to claim 1 , wherein the percarbonate or persulphate bleach comprises sodium or potassium percarbonate or persulphate.4. The method according to claim 1 , wherein the organic peracid comprises a perbenzoic acid and/or a peroxycarboxylic acid.5. The method according to claim 4 , wherein the peroxycarboxylic acid comprises monoperoxyphthalic acid claim 4 , diperoxyphthalic acid claim 4 , 2-octyldiperoxysuccinic acid claim 4 , diperoxydodecanedicarboxylic acid claim 4 , diperoxy-azelaic acid claim 4 , ...

Polypeptides Having Peroxygenase Activity and Polynucleotides Encoding Same

The present invention relates to isolated polypeptides having peroxygenase 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.

TABLET BINDING COMPOSITIONS

Provided are tablet binding compositions for binding cleaning and/or disinfecting formulation components into tablets. The tablet binding compositions are suitable replacements for traditional tablet binder compounds, such as boric acid or zeolites. The tablet binding compositions provided herein can produce tablets of increased hardness at lower compression forces and, when dissolved, yield solutions of increased clarity compared to some traditional binder compounds. Also provided are processes for preparing the tablet binding compositions and methods for formation of tablets containing the tablet binding compositions. 1. A tablet binding composition , comprising:an acetate salt, having a particle size distribution such that at least 70% of the particles are greater than 150 μm, and present in an amount of from about 15% to about 85% by weight of the composition; anda C6 saccharide derivative sequestrant selected from among an amino hexose, hexitol, aldonic acid, aldonic acid lactone, hexose-delta-lactone, and saccharic acid and a salt of any of these compounds and a combination thereof, having a particle size distribution such that at least 70% of the particles are greater than 150 μm, and present in an amount of from about 15% to about 85% by weight of the composition,wherein the ratio of the acetate salt to the C6 saccharide derivative sequestrant is in the range of about 5:1 to about 1:5.2. The tablet binding composition of claim 1 , wherein the acetate salt is selected from among sodium acetate claim 1 , potassium acetate claim 1 , calcium acetate claim 1 , magnesium acetate claim 1 , silver acetate and a combination thereof.4. A tablet claim 1 , comprising:{'claim-ref': {'@idref': 'CLM-00001', 'claim 1'}, 'a tablet binding composition of in an amount of from about 0.5% to about 25% by weight of the tablet; and'}an ingredient selected from among an enzyme, a bleaching agent, sodium perborate, sodium percarbonate, an expanded sodium percarbonate, an expanded ...

LAUNDRY DETERGENT COMPOSITIONS COMPRISING RENEWABLE COMPONENTS

The present disclosure relates to detergent compositions that comprise renewable components and exhibit good performance, as compared to both traditional detergent formulations that contain non-renewable ingredients and known detergent formulations that contain renewable components. 1. A laundry detergent composition comprising: from about 1% to about 20% by weight of alkyl ether sulfate of the formula R—(OCHCH)—O—SOM , wherein Ris a non-petroleum derived , linear or branched fatty alcohol consisting of even numbered carbon chain lengths of from about Cto about C , and wherein x is from about 0.5 to about 8 , and where M is an alkali metal or ammonium cation; from about 1% to about 15% by weight of fatty alcohol ethoxylate of formula R—(OCHCH)—OH , wherein Ris a non-petroleum derived , linear or branched fatty alcohol consisting of even numbered carbon chain lengths of from about Cto about C , and wherein y is from about 0.5 to about 15; from about 0.1% to about 5% by weight of amine oxide; from about 0.1% to about 5% of a cleaning polymer , from about 1% to about 15% by weight of a solvent comprising 1 ,2-propanediol; and water , wherein the composition is substantially free of dye and brightener.2. The laundry detergent composition of wherein the laundry detergent composition comprises a polyhydric alcohol selected from the group consisting of 2 claim 1 ,3-butanediol claim 1 , 2 claim 1 ,3-pentanediol claim 1 , 2 claim 1 ,4-pentanediol claim 1 , 1 claim 1 ,2-butanediol claim 1 , 2 claim 1 ,3-hexandiol claim 1 , 1 claim 1 ,5-pentanediol claim 1 , and mixtures thereof.3. The laundry detergent composition of wherein the composition comprises from about 0.01% to about 0.1% of a polyhydric alcohol.4. The laundry detergent composition of wherein the composition comprises from about 0.01% to about 0.1% of 2 claim 1 ,3-hexandiol.5. The laundry detergent composition of wherein the composition is substantially free of linear or branched alkyl benzene sulfonates.6. The ...

HEAVY DUTY LAUNDRY DETERGENT

A laundry detergent formulation is provided that is formed as an aqueous blend of surfactants, enzymes, builders, and soil release polymers to inhibit soil re-deposition back onto other clothing or elements of the washing machine. The detergent formulation also contains additives with properties that impart a treatment to fabrics that inhibits future soil deposition onto the clothing with continued use. The detergent formulation provides cleaning of heavy duty grease and automotive soils from clothing surfaces that is superior to current detergent products. 1. A process for cleaning clothing having soil thereon in a washing machine comprising: one or more builders;', 'one or more enzymes;', 'one or more surfactants;', 'a biocide;', 'a soil release polymer of a nonionic oligoester_present from 0.6 to 5.5 total weight percent; and', 'allowing sufficient time for the pre-spotter formulation to clean the clothing during operation of the washing machine without redeposition of the soil back onto the clothing or the washing machine once the soil is removed from the clothing., 'applying a pre-spotter formulation to a spot or a stain to be removed from an article of clothing prior to insertion into the washing machine, the pre-spotter formulation comprising2. The process of wherein the formulation is monophasic for at least 4 months storage at 20° Celsius as measured by a change of less than one pH unit.3. The process of wherein the one or more builders further comprises sodium citrate.4. The process of wherein said one or more builders further comprises at least one of borax or ethanolamine.5. The process of wherein said one or more enzymes comprises cellulase.6. The process of wherein said one or more surfactants comprises at least one of alkylbenzene sulfonate claim 1 , alkyldiphenyl disulfonate claim 1 , or linear alcohol ethoxylate.7. The process of wherein said solvent further comprises an ester solvent.8. The process of wherein said solvent further comprises a ...

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 ...

Polypeptides Having Laccase Activity and Polynucleotides Encoding Same

The present invention relates to isolated polypeptides having laccase activity and polynucleotides encoding the polypeptides 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.

AMPHIPHILIC POLYSACCHARIDE DERIVATIVES AND COMPOSITIONS COMPRISING SAME

The disclosure relates to compositions comprising a polysaccharide derivative, wherein the polysaccharide derivative comprises a polysaccharide substituted with a) at least one hydrophobic group, and b) at least one hydrophilic group, wherein the polysaccharide is poly alpha-1,3-glucan, poly alpha-1,6-glucan, or poly alpha-1,3-1,6-glucan. 1. A composition comprising:a polysaccharide derivative, wherein the polysaccharide derivative comprises a polysaccharide substituted witha) at least one hydrophobic group; andb) at least one hydrophilic group;wherein the polysaccharide is poly alpha-1,3-glucan, poly alpha-1,6-glucan, or poly alph-1,3-1,6-glucan.2. The composition of claim 1 , wherein the poly alpha-1 claim 1 ,3-glucan comprises a backbone of glucose monomer units wherein greater than or equal to 50% of the glucose monomer units are linked via alpha-1 claim 1 ,3-glycosidic linkages.3. The composition of claim 1 , wherein the poly alpha-1 claim 1 ,3-glucan comprises a backbone of glucose monomer units wherein greater than or equal to 90% of the glucose monomer units are linked via alpha-1 claim 1 ,3-glycosidic linkages.4. The composition of claim 1 , wherein the poly alpha-1 claim 1 ,6-glucan comprises a backbone of glucose monomer units wherein greater than or equal to 40% of the glucose monomer units are linked via alpha-1 claim 1 ,6-glycosodic linkages.5. The composition of claim 1 , wherein the poly alpha-1 claim 1 ,6-glucan has a degree of alpha-1 claim 1 ,2-branching that is less than 50%.6. The composition of claim 1 , wherein the at least one hydrophobic group comprises a Cto Calkyl claim 1 , a Cto Calkene claim 1 , a Cto Calkyne claim 1 , a polyether comprising repeat units of (—CHCHO—) claim 1 , (—CHCH(CH)O—) claim 1 , or mixtures thereof claim 1 , wherein the total number of repeat units is in the range of from 3 to 100 claim 1 , a Cto Caryl claim 1 , a benzyl claim 1 , a C-Calkyl sulfonyl claim 1 , a C-Caryl sulfonyl claim 1 , a p-toluenesulfonyl group ...

COMPOSITIONS FOR TREATMENT AND METHODS FOR MAKING AND USING THE SAME

A detergent composition, a method of making the detergent composition, and a method of use thereof are provided. The detergent composition comprises at least 0.001% by weight of an antimicrobial agent, based on the total weight of the composition; an enzyme; and at least 0.01% by weight of a hydrotrope, based on the total weight of the composition. 1. A detergent composition comprising:at least 0.001% by weight of an antimicrobial agent, based on the total weight of the composition;an enzyme; andat least 0.01% a hydrotrope, based on the total weight of the composition.2. The composition of claim 1 , wherein the hydrotrope comprises an anionic hydrotrope.3. The composition of claim 2 , wherein the anionic hydrotrope comprises at least one of an alkanoic acid claim 2 , an aromatic sulfonic acid claim 2 , an aromatic carboxylic acid claim 2 , and a salt of any thereof.4. The composition of claim 3 , wherein the aromatic sulfonic acid is at least one of xylene sulfonic acid claim 3 , cumene sulfonic acid claim 3 , and a salt of any thereof.5. The composition of claim 1 , comprising 0.1% or less by weight of a boron-containing compound claim 1 , based on the total weight of the composition.6. The composition of claim 1 , comprising either no boron-containing compound or only an incidental amount.7. The composition of claim 1 , wherein the antimicrobial agent comprises at least one of a biguanide compound and a quaternary ammonium compound.8. The composition of claim 7 , wherein the biguanide compound comprises at least one of chlorhexidine and a salt thereof.9. The composition of claim 1 , wherein the enzyme comprises at least one of a lipase claim 1 , a protease claim 1 , a peptidase claim 1 , an amylase claim 1 , a glycosidase claim 1 , a cellulase claim 1 , DNAse and a nuclease.10. The composition of claim 1 , wherein the composition has a pH in a range of 6 to 11.11. The composition of claim 1 , further comprising at least one of:at least 0.0001% by weight of a ...

CLEANING COMPOSITIONS COMPRISING ESTERAMINES

Cleaning compositions that include esteramines. Related methods of preparation and use. 2. A composition according to claim 1 , wherein{'sup': '1', 'sub': 4', '30, 'Ris C-C-alkyl, and'}{'sup': '2', 'sub': 3', '12, 'Ris C-C-alkylene.'}3. A composition according to claim 1 , wherein{'sup': '1', 'sub': 6', '21, 'Ris C-C-alkyl, and'}{'sup': '2', 'sub': 3', '6, 'Ris C-C-alkylene.'}4. The composition according to claim 1 , wherein{'sup': 1', '1, 'sub': 6', '21', '8', '12, 'i) Ris a mixture of at least two individual substituents, preferably Ris a mixture of at least two C-C-alkyl substituents, more preferably of at least two C-C-alkyl substituents, and/or'}{'sup': '1', 'sub': 4', '30', '4', '30', '6', '21', '8', '12, 'ii) Ris unsubstituted straight-chain or branched C-C-alkyl or C-C-alkenyl, preferably unsubstituted straight-chain or branched C-C-alkyl, more preferably unsubstituted straight-chain or branched C-C-alkyl.'}5. The composition according to any claim 1 , wherein{'sup': '2', 'sub': 2', '12', '3', '6, 'i) Ris straight-chain C-C-alkylene, preferably straight-chain C-C-alkylene, or'}{'sup': 2', '7', '9', '11', '5', '7, 'sub': 2', 'm', '2', 'o', '2', '3', '2', '2', 'p', '2', '2', 'r, 'claim-text': [{'sup': 5', '7', '9', '11', '5', '7', '9', '11, 'R, R, Rand Rare independently of each other selected from H or methyl, preferably R, R, Rand Rare H,'}, 'm is an integer from 1 to 10, preferably m is 1,', 'n is an integer from 2 to 6, preferably n is 2,', 'o is an integer from 0 to 5, preferably o is 0 or 1,', 'p is an integer from 1 to 3, preferably p is 1, and', 'r is an integer from 1 to 3, preferably r is 1., 'ii) Ris —(CH—CHR—O)—CH—CHR—, —(CHR)—CHR—CHR—O—(CH)— or —(CH—CH)—O—(CH—CH)—,'}6. The composition according to claim 1 , wherein the composition comprises a salt of the esteramine according to claim 1 , wherein the salt is formed by at least partial protonation of the amine group by an acid being a protic organic or inorganic acid.7. A cleaning composition ...

Process

A method of providing a modifier on the surface of an active-containing core-shell aminoplast microcapsule, including the covalent attachment of the modifier to the capsule shell surface by means of a coupling compound capable of covalent bonding to both shell and modifier by means of epoxy groups on the coupling compound. The method is especially useful for enhancing the substantiveness to fabrics of fragrance microcapsules added to laundry products. 1. A method of providing a modifier on the surface of an active-containing core-shell aminoplast microcapsule , comprising the covalent attachment of the modifier to the capsule shell surface by means of a coupling compound capable of covalent bonding to both shell and modifier by means of epoxy groups on the coupling compound.2. The method according to claim 1 , in which the shell is of melamine-formaldehyde resin.3. The method according to claim 1 , in which the modifier is selected from a polysaccharide and an enzyme.4. The method according to claim 3 , in which the enzyme is a lipase.5. The method according to claim 1 , in which the coupling compound is poly(ethylene glycol) diglycidyl ether having an Mof from 300-10 claim 1 ,000.6. The method according to claim 1 , in which the coupling compound is glycidyl methacrylate.7. The method according to claim 6 , in which the epoxy group of the glycidyl methacrylate is first reacted with the aminoplast of the shell claim 6 , and free-radical addition polymerisation is then initiated with other glycidyl methacrylate molecules claim 6 , to provide a plurality of epoxy groups.8. The method according to claim 1 , in which the coupling compound is first attached covalently to the shell claim 1 , and subsequently is covalently attached to the modifier.9. The method according to claim 1 , in which the coupling compound is first attached covalently to the modifier claim 1 , and subsequently is covalently attached to the shell.10. The method according to in which the modifier is ...

DNASE VARIANTS

The present invention relates to polypeptide variants and methods for obtaining 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 DNase variant , comprising an substitution at one or more positions corresponding to positions 4 , 17 , 19 , 36 , 38 , 40 , 41 , 45 , 51 , 53 , 54 , 55 , 57 , 64 , 66 , 67 , 68 , 69 , 70 , 71 , 72 , 74 , 75 , 77 , 82 , 83 , 84 , 85 , 86 , 88 , 91 , 99 , 101 , 105 , 105 , 106 , 115 , 116 , 135 , 136 , 138 , 139 , 140 , 141 , 151 , 152 , 153 , 154 , 162 , 163 , 164 , 166 , 168 , 169 , 173 , 182 , 183 , 184 , 185 , 186 , 189 , 189 , 212 , and 215 of SEQ ID NO: 1 , wherein the variant has a sequence identity to the polypeptide shown in SEQ ID NO: 1 of at least 80% , wherein the variant has DNase activity and wherein the variant has improved stability as compared to the SEQ ID NO 1.2. The DNase variant of claim 1 , wherein the variant comprises one or more substitutions selected from the group consisting of N4E claim 1 , L17E claim 1 , T19A claim 1 , T19G claim 1 , T19I claim 1 , K36P claim 1 , Q38P claim 1 , A40P claim 1 , A40H claim 1 , L41T claim 1 , L41H claim 1 , V45H claim 1 , L51G claim 1 , K53T claim 1 , K53P claim 1 , G54P claim 1 , A55P claim 1 , N57H claim 1 , E64A claim 1 , E64Q claim 1 , E64R claim 1 , E64T claim 1 , E64I claim 1 , E64S claim 1 , T66H claim 1 , K67A claim 1 , K67T claim 1 , N68V claim 1 , N68P claim 1 , N68I claim 1 , N68H claim 1 , S69A claim 1 , S69D claim 1 , S69E claim 1 , S69K claim 1 , S69L claim 1 , S69W claim 1 , S69Y claim 1 , S69Q claim 1 , N70T claim 1 , N70H claim 1 , N70G claim 1 , R71T claim 1 , D72E claim 1 , S74H claim 1 , S74G claim 1 , G75I claim 1 , N77T claim 1 , K82P claim 1 , K82I claim 1 , D83T claim 1 , D83P claim 1 , D83I claim 1 , D83H claim 1 , D83G claim 1 , P84H claim 1 , Q85T claim 1 , Q85P claim 1 , Q85H claim 1 , K86T claim 1 , ...

Automatic dishwashing detergent composition

An automatic dishwashing cleaning composition comprising: a) a mixed builder system comprising soluble builder and crystalline silicate wherein the soluble builder comprises a complexing agent, a phosphonate and a dispersant polymer and wherein the level of each soluble builder in the composition is: a1) from 15% to 40% by weight of the composition of the complexing agent; a2) from 2% to 7% by weight of the composition of the phosphonate; and a3) from 1% to 7% by weight of the composition of the dispersant polymer wherein the soluble builder and the crystalline silicate are in a weight ratio of from 8:1 to 15:1 b) a bleaching system comprising bleach, a bleach catalyst and a bleach activator; and c) from 0% to 20% by weight of the composition of carbonate.

Microencapsulation Using Amino Sugar Oligomers

The present invention provides a microcapsule composition produced by crosslinking of oligomers comprising amino sugars, which is used for stabilizing detergent components. 1. A microcapsule composition , comprising a compound entrapped in an aqueous compartment formed by a membrane , wherein the membrane surrounds the compartment and comprises cross-linked amino sugar oligomers.2. The composition of claim 1 , wherein the compound is a detergent enzyme.3. The composition of claim 2 , wherein the detergent enzyme is selected from the group consisting of protease claim 2 , metalloprotease claim 2 , subtilisin claim 2 , amylase claim 2 , lipase claim 2 , cutinase claim 2 , cellulase claim 2 , mannanase claim 2 , pectinase claim 2 , xanthanase claim 2 , DNase claim 2 , laccase claim 2 , peroxidase claim 2 , haloperoxidase claim 2 , perhydrolase claim 2 , and combinations thereof.4. The composition of claim 2 , wherein the compartment contains at least 1% active enzyme by weight of the total compartment.5. The composition of claim 1 , wherein the diameter of the compartment is at least 50 micrometers.6. The composition of claim 1 , which further includes an alcohol.7. The composition of claim 1 , wherein the amino sugar oligomers comprise at least 60% w/w of amino sugar monomers.8. The composition of claim 1 , wherein the amino sugar oligomers comprise at least 60% w/w of glucosamine monomers.9. The composition of claim 1 , wherein the amino sugar oligomers are chitosan oligomers.10. The composition of claim 1 , wherein the amino sugar oligomers are composed of randomly distributed β(1→4)-linked glucosamine and N-acetyl-glucosamine.11. The composition of claim 1 , wherein the amino sugar oligomers have a weight average molecular weight (M) of 300 to 15000 Daltons.12. The composition of claim 1 , wherein the amino sugar oligomers have a weight average molecular weight (M) of 300 to 5000 Daltons.13. The composition of claim 1 , wherein the membrane is produced by using an ...

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 ...

GENES ENCODING CELLULASE

Polynucleotide sequences are provided encoding a thermostable cellulase and directing its increased expression are provided, and the use of the thermostable cellulase in hydraulic fracturing methods and the treatment of flowback fluids. 1. A nucleotide sequence of SEQ ID NO:1. This application is a divisional of U.S. application Ser. No. 14/389,339, which is the United States National Phase filing of International Application No.: PCT/US2013/030527, filed Mar. 12, 2013, which designated the United States, was published in English and claims priority of U.S. Provisional Applications 61/618,610, filed Mar. 30, 2012 and 61/704,368, filed Sep. 21, 2012. The contents of the aforementioned applications are hereby expressly incorporated by reference in their entireties.Polynucleotide sequences encoding a cellulase are provided. In particular, the polynucleotide sequences may provide increased expression of a specific, thermostable, thermotolerant, pressure stable enzyme such as a cellulase.This application is being filed electronically via the USPTO EFS-WEB server, as authorized and set forth in MPEP § 502.05 and this electronic filing includes an electronically submitted sequence listing; the entire content of this sequence listing is hereby incorporated by reference into the specification of this application. The sequence listing is identified on the electronically filed ASCII (.txt) text file as follows:O-Glycosyl hydrolases (EC 3.2.1.-) are a widespread group of naturally-occurring enzymes that hydrolyze the glycosidic bond between two or more carbohydrates or between a carbohydrate and a non-carbohydrate moiety. The International Union of Biochemistry and Molecular Biology (IUBMB) enzyme nomenclature of glycosyl hydrolases (or glycosylases) is based principally on their substrate specificity and occasionally on their molecular mechanism (Nomenclature Committee of the International Union of Biochemistry and Molecular Biology (NC-IUBMB), Accessed Oct. 24, 2011).IUBMB ...

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 , ...

Pectinases with Improved Thermostability

The invention is in the field of protein chemistry, in particular in the field of enzymology. It provides pectinases, i.e. polypeptides with pectin-degrading properties. In particular the invention provides polypeptides with pectate lyase activity (EC 4.2.2.2). Enzymes according to the invention have improved properties, such as improved thermostability and decreased calcium dependence. 1. A polypeptide with pectate lyase activity , the polypeptide comprising:an amino acid sequence that is at least 70% identical to the amino acid according to SEQ ID NO: 1, anda small, polar, non-charged amino acid residue at an amino acid position corresponding to position 235 in SEQ II) NO: 1, andwherein the polypeptide has an improved thermostability.2. The polypeptide claim 1 , wherein the small claim 1 , polar claim 1 , non-charged amino acid residue is selected from the group consisting of amino acids Threonine claim 1 , Serine claim 1 , Asparagine and Cysteine.3. The polypeptide of claim 1 , wherein the small claim 1 , polar claim 1 , non-charged amino acid residue is Threonine.4. The polypeptide of claim 1 , wherein the polypeptide comprises an amino acid sequence that is at least 75% identical to the amino acid according to SEQ ID NO: 1.5. The polypeptide of claim 1 , wherein the polypeptide comprises a leucine residue at an amino acid position corresponding to position 231 in SEQ ID NO: 1.6. (canceled)7. A composition comprising the polypeptide of .8. A nucleic acid encoding the polypeptide of .9. A vector comprising the nucleic acid of .10. A composition comprising the nucleic acid of .11. A recombinant host cell comprising acid of .12Escherichia coli, Bacillus, Corynebacterium, Pseudomonas, Pichia pastoris, Saccharomyces cerevisiae, Yarrowia lipolytica,. The recombinant host cell of claim 11 , wherein the host cell is selected from the group consisting of filamentous fungi claim 11 , yeast and insect cells.13. A method for producing the polypeptide of claim 1 , the method ...

GH61 Polypeptide Variants and Polynucleotides Encoding Same

The present invention relates to GH61 polypeptide 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 GH61 polypeptide variant , comprising a substitution at one or more positions corresponding to positions 105 , 154 , 188 , 189 , 216 , and 229 of the mature polypeptide of SEQ ID NO: 30 , wherein the variant has cellulolytic enhancing activity.2. The variant of claim 1 , which has at least 60% claim 1 , at least 65% claim 1 , at least 70% claim 1 , at least 75% claim 1 , at least 80% claim 1 , at least 81% claim 1 , at least 82% claim 1 , at least 83% claim 1 , at least 84% claim 1 , at least 85% claim 1 , at least 86% claim 1 , at least 87% claim 1 , at least 88% claim 1 , at least 89% claim 1 , at least 90% claim 1 , at least 95% claim 1 , at least 96% claim 1 , at least 97% claim 1 , at least 98% claim 1 , or at least 99% claim 1 , but less than 100% claim 1 , sequence identity to the amino acid sequence of a parent GH61 polypeptide.3. The variant of any of claims 1 , which is a variant of a parent GH61 polypeptide selected from the group consisting of: (a) a polypeptide having at least 60% sequence identity to the mature polypeptide of SEQ ID NO: 2 claims 1 , 4 claims 1 , 6 claims 1 , 8 claims 1 , 10 claims 1 , 12 claims 1 , 14 claims 1 , 16 claims 1 , 18 claims 1 , 20 claims 1 , 22 claims 1 , 24 claims 1 , 26 claims 1 , 28 claims 1 , 30 claims 1 , 32 claims 1 , 34 claims 1 , 36 claims 1 , 38 claims 1 , 40 claims 1 , 42 claims 1 , 44 claims 1 , 46 claims 1 , 48 claims 1 , 50 claims 1 , 52 claims 1 , 54 claims 1 , 56 claims 1 , 58 claims 1 , 60 claims 1 , 62 claims 1 , 64 claims 1 , 66 claims 1 , 68 claims 1 , 70 claims 1 , 72 claims 1 , 74 claims 1 , 76 claims 1 , 78 claims 1 , 80 claims 1 , 82 claims 1 , 84 claims 1 , 86 claims 1 , 88 claims 1 , 90 claims 1 , 92 claims 1 , 94 claims 1 , 96 claims 1 , 98 ...

Low pH Powder Detergent Composition

The invention relates to low pH powder detergent composition comprising at least one polypeptide having alpha-amylase activity and at least 60%, such as 65%, such as 70%, such as 75%, such as 80%, such as 85%, such as 90%, such as 95%, such as 97% sequence identity to SEQ ID NOs: 1-19 and the composition has a pH value below 9.5. 1. A powder detergent composition comprising at least one polypeptide having alpha-amylase activity and at least 60% , but less than 100% sequence identity to SEQ ID NOs: 1-19 , wherein the composition has a pH value below 9.5 , wherein pH is determined in a 5 g/l solution of the composition in deionized water at 20° C.2. The composition according to claim 1 , wherein the pH is in the range of 7.0-9.5; such as in the range of 7.5 to 9.0; such as in the range of 8.0 to 9.0.3. The composition of claim 1 , wherein the polypeptide having alpha-amylase activity has at least 60% claim 1 , at least 65% claim 1 , at least 70% claim 1 , at least 75% claim 1 , at least 80% claim 1 , at least 85% claim 1 , at least 90% or at least 95% but less than 100% sequence identity to SEQ ID NOs: 1-19.4. The composition of claim 1 , wherein the composition further comprises one or more detergent components.5. The composition of claim 4 , wherein detergent components selected from the group consisting of surfactants claim 4 , hydrotropes claim 4 , builders claim 4 , co-builders claim 4 , chelators or chelating agents claim 4 , bleaching system or bleach components claim 4 , polymers claim 4 , fabric hueing agents claim 4 , fabric conditioners claim 4 , foam boosters claim 4 , suds suppressors claim 4 , dispersants claim 4 , dye transfer inhibitors claim 4 , fluorescent whitening agents claim 4 , perfumes claim 4 , optical brighteners claim 4 , bactericides claim 4 , fungicides claim 4 , soil suspending agents claim 4 , soil release polymers claim 4 , anti-redeposition agents claim 4 , enzyme inhibitors or stabilizers claim 4 , enzyme activators claim 4 , ...

TRIAMINE SOLIDIFICATION USING DIACIDS

Stable, solid triamine compositions are disclosed. The pressed, cast, extruded or other solid compositions are suitable for antimicrobial, sanitizing and disinfectant applications. Ready-to-use solutions are obtained by dissolving the solid triamine compositions with water and the methods of use thereof are particularly suitable for cleaning, disinfecting, sanitizing, rinsing and/or lubricating. Beneficially, the solid triamine compositions are at least partially neutralized, allowing activity of 90% and greater of the biocidal triamine, and provide at least substantially similar or superior performance and micro efficacy to liquid formulations. 120-. (canceled)21: A solid triamine composition comprising: [{'br': None, 'sub': 2', 'r', 'y', '2', 'm', '2, 'R—NH—[(CH)NH]—(CH)—NH'}, {'br': None, 'sub': 2', 'r', '2', '2, 'R—N[(CH)NH]'}, 'wherein:', 'R is a linear or branched alkyl residue with 1 to 22 carbon atoms,', 'm, r, and y independently represent an integer ranging from 1 to 6; and, 'a triamine comprising any one of the following formulasa diacid comprising acetic acid, adipic acid, aspartic acid, dipicolinic acid, malic acid, malonic acid, oxalic acid, succinic acid, or tartaric acid or combinations thereof;wherein the ratio of the diacid to the triamine is from about 1:10 to about 1:1, andwherein the combination of the triamine and diacid forms an at least partially neutralized solid matrix; andwherein the composition remains solid below about 50° C. without casting or extrusion.22: The composition of claim 21 , further comprising an enzyme and/or a chelant.23: The composition of claim 22 , wherein the enzyme is a lipase.24: The composition of claim 21 , further comprising at least one functional ingredient selected from the group consisting of: surfactants claim 21 , chelating agents claim 21 , sequestering agents claim 21 , detergents claim 21 , alkaline sources claim 21 , builders claim 21 , rinse aids claim 21 , hardening agents claim 21 , bleaching agents ...

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.

Polypeptides With Lipase Activity and Polynucleotides Encoding Same

The present invention relates to isolated polypeptides with lipase activity, selected from the group consisting of: (a) a polypeptide having at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to SEQ ID NO: 4; (b) a polypeptide encoded by a polynucleotide that hybridizes under low stringency conditions, medium stringency conditions, medium-high stringency conditions, high stringency conditions, or very high stringency conditions with (i) SEQ ID NO: 3 or the full-length complement of (i); (c) a polypeptide encoded by a polynucleotide having at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to SEQ ID NO: 3; (d) a polypeptide which is a variant of SEQ ID NO: 4 comprising a substitution, deletion, and/or insertion at one or more (e.g. several) positions; and (e) a polypeptide which is a fragment of any of the polypeptides of (a), (b), (c) or (d). The invention also relates to polynucleotides encoding the polypeptides; nucleic acid constructs, vectors, and host cells comprising the polynucleotides; and methods of using the polypeptides. 124-. (canceled)25. An isolated polypeptide with lipase activity , selected from the group consisting of:(a) a polypeptide having at least 75% sequence identity to SEQ ID NO: 4;(b) a polypeptide encoded by a polynucleotide that hybridizes under low stringency conditions, medium stringency conditions, medium-high stringency conditions, high stringency conditions, or very high stringency conditions with (i) SEQ ID NO: 3 or the full-length complement of (i);(c) a polypeptide encoded by a polynucleotide having at least 75% sequence identity to SEQ ID NO: 3;(d) a polypeptide which is a variant of SEQ ID NO: 4 comprising a substitution, ...

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 ...

OXYGEN-BASED CLEANING COMPOSITION

An oxygen-based cleaning composition, comprises a cleaning formulation in powder form, wherein the cleaning formulation includes a hydrogen peroxide addition compound layer comprising a hydrogen peroxide addition compound powder for producing hydrogen peroxide, a surfactant layer formed by coating an outer surface of the hydrogen peroxide addition compound layer with a liquid surfactant, and a saponin layer formed by coating an outer surface of the surfactant layer with a saponin powder. 1. An oxygen-based cleaning composition , comprising a cleaning formulation in powder form ,wherein the cleaning formulation includes a hydrogen peroxide addition compound layer comprising a hydrogen peroxide addition compound powder for producing hydrogen peroxide, a surfactant layer formed by coating an outer surface of the hydrogen peroxide addition compound layer with a liquid surfactant, and a saponin layer formed by coating an outer surface of the surfactant layer with a saponin powder.2. The oxygen-based cleaning composition of claim 1 , wherein the cleaning formulation further includes a sodium bicarbonate layer formed by coating an outer surface of the saponin layer with a sodium bicarbonate powder.3. The oxygen-based cleaning composition of claim 2 , wherein the cleaning formulation comprises claim 2 , based on 100 parts by weight of the hydrogen peroxide addition compound claim 2 , 8 to 13 parts by weight of the surfactant claim 2 , 0.5 to 2 parts by weight of saponin claim 2 , and 4 to 8 parts by weight of sodium bicarbonate.4. The oxygen-based cleaning composition of claim 2 , wherein the cleaning formulation further includes a binder layer applied on an outer surface of the sodium bicarbonate layer and a yeast layer applied on an outer surface of the binder layer.5. The oxygen-based cleaning composition of claim 2 , wherein the saponin is saponin extracted from soapberries.6. The oxygen-based cleaning composition of claim 4 , wherein the hydrogen peroxide addition ...

METHODS AND COMPOSITIONS FOR REDUCING PERSISTENT ODOR IN CLOTHING AND MITIGATING BIOFILMS

Novel methods and compositions for treating textiles and other materials are disclosed in which persistent odor or other symptoms of biofilm presence can be reduced through the use of compositions comprising a biofilm attack agent such as N-acetyl cysteine or certain enzymes, coupled with surfactants and other agents. 1. A method for treating a textile item having or suspected of having biofilm matter in one or more regions associated with persistent odor , the method comprising applying an enzymatic composition to the one or more regions having biofilm matter , providing suitable time for the enzymatic mixture to attack the biofilm , and then washing the textile item , wherein the enzymatic composition comprises: (a) water , (b) from 5% to 60% of a surfactant , (c) from 1% to 20% of an enzyme mixture comprising at least two of lysozyme , proteinase , amylase , mannanase , lipase , pectinase , DNAse and cellulase; and (d) from 0.1% to 10% of N-acetyl cysteine.2. The method of claim 1 , wherein the enzymatic composition further comprises from 0.01% to 8% by weight of bacterial spores adapted to become active in response to the presence of contaminants on textiles selected from at least one of proteins claim 1 , carbohydrates claim 1 , lipids claim 1 , and carbohydrates claim 1 , the spores then producing enzymes that attack a portion of said contaminants.3. The method of claim 2 , wherein the concentration of the bacterial spores is between 1×10and 5×10colony forming units per ml.4. The method of claim 1 , wherein the enzymatic composition is packaged with indicia instructing a user to wait at least 5 minutes between applying the enzymatic composition and washing the textile claim 1 , wherein washing comprises washing in water with a laundry detergent.5. The method of claim 1 , wherein the enzymatic composition comprises at least two portions claim 1 , a first portion comprising an enzyme mixture and a second portion comprising N-acetyl cysteine claim 1 , further ...

Enzymatic process for producing intermediates useful as esterquat precursors

The invention provides a process for the preparation of a modified triethanolamine/fatty acid ester composition ratio by treatment of a conventional tnethanolamine fatty acid ester composition with a hydrolytic enzyme. Also provided are novel mixtures of tnethanolamine and mono-, di-, and tri-esters of fatty acids which are useful in the preparation of cationic surfactants useful in fabric softening applications. In one aspect, the method increases the triester fraction without significantly affecting the amount of mono-ester and unesterified species, which in turn adds to the flexibility in the formulation of the corresponding fabric softening compositions.