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Небесная энциклопедия

Космические корабли и станции, автоматические КА и методы их проектирования, бортовые комплексы управления, системы и средства жизнеобеспечения, особенности технологии производства ракетно-космических систем

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Мониторинг СМИ

Мониторинг СМИ и социальных сетей. Сканирование интернета, новостных сайтов, специализированных контентных площадок на базе мессенджеров. Гибкие настройки фильтров и первоначальных источников.

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Поддерживает ввод нескольких поисковых фраз (по одной на строку). При поиске обеспечивает поддержку морфологии русского и английского языка
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Применить Всего найдено 14385. Отображено 100.
02-02-2012 дата публикации

Preparation of adipic acid

Номер: US20120028320A1
Автор: Axel Christoph Trefzer, Martin SCHÜRMANN, Petronella Catharina Raemakers-Franken, Stefaan Marie Andre De Wildeman
Принадлежит: DSM IP ASSETS BV

The invention relates to a method for preparing adipic acid, comprising converting alpha-ketoglutaric acid (AKG) into alpha-ketoadipic acid (AKA), converting alpha-ketoadipic acid into alpha-ketopimelic acid (AKP), converting alpha-ketopimelic acid into 5-formylpentanoic acid (5-FVA), and converting 5-formylpentanoic acid into adipic acid, wherein at least one of these conversions is carried out using a heterologous biocatalyst.The invention further relates to a heterologous cell, comprising one or more heterologous nucleic acid sequences encoding one or more heterologous enzymes capable of catalysing at least one reaction step in said method.

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Номер записи: 1
02-02-2012 дата публикации

Methods of increasing dihydroxy acid dehydratase activity to improve production of fuels, chemicals, and amino acids

Номер: US20120028322A1
Автор: Andrew Hawkins, Aristos Aristidou, Catherine Asleson Dundon, Doug Lies, Lynne H. Albert
Принадлежит: Gevo Inc

The present invention is directed to recombinant microorganisms comprising one or more dihydroxyacid dehydratase (DHAD)-requiring biosynthetic pathways and methods of using said recombinant microorganisms to produce beneficial metabolites derived from said DHAD-requiring biosynthetic pathways. In various aspects of the invention, the recombinant microorganisms may be engineered to overexpress one or more polynucleotides encoding one or more Aft proteins or homologs thereof. In some embodiments, the recombinant microorganisms may comprise a cytosolically localized DHAD enzyme. In additional embodiments, the recombinant microorganisms may comprise a mitochondrially localized DHAD enzyme. In various embodiments described herein, the recombinant microorganisms may be microorganisms of the Saccharomyces Glade, Crabtree-negative yeast microorganisms, Crabtree-positive yeast microorganisms, post-WGD (whole genome duplication) yeast microorganisms, pre-WGD (whole genome duplication) yeast microorganisms, and non-fermenting yeast microorganisms.

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Номер записи: 2
21-06-2012 дата публикации

Preparation of alpha-ketopimelic acid

Номер: US20120156737A1
Автор: Axel Christoph Trefzer, Martin SCHÜRMANN, Petronella Catharina Raemakers-Franken, Stefaan Marie Andre De Wildeman
Принадлежит: DSM IP ASSETS BV

The invention relates to a method for preparing alpha-ketopimelic acid, comprising converting alpha-ketoglutaric acid into alpha-ketoadipic acid and converting alpha-ketoadipic acid into alpha-ketopimelic acid, wherein at least one of these conversions is carried out using a heterologous biocatalyst. The invention further relates to a heterologous cell, comprising one or more heterologous nucleic acid sequences encoding one or more heterologous enzymes capable of catalysing at least one reaction step in the preparation of alpha-ketopimelic acid from alpha-ketoglutaric acid.

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Номер записи: 3
12-07-2012 дата публикации

System for producing l-homophenylalanine and a process for producing l-homophenylalanine

Номер: US20120178133A1
Автор: Abdul Latif Ahmad, Pei Ching Oh, Syamsul Rizal Abd. Shukor
Принадлежит: Universiti Sains Malaysia (USM)

The present invention relates to a system ( 10 ) for producing L-homophenylalanine and a process for producing L-homophenylalanine using the system ( 10 ). The system ( 10 ) and the process include monitoring and controlling of the reaction conditions (e.g., temperature and pH) to desired or predetermined values. The monitoring, adjusting and agitating steps provided by the method thereby result in a more complete conversion of the available substrate and produce a sufficient yield of homophenylalanine.

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Номер записи: 4
26-07-2012 дата публикации

Microorganism producing o-phosphoserine and method of producing l-cysteine or derivatives thereof from o-phosphoserine using the same

Номер: US20120190083A1
Автор: Byeong Cheol Song, Eun Bin YANG, Hye Won Kim, Hye Won Um, Hyun Ae Bae, Jae Hyun Jo, Jin Sook CHANG, Kyoung Min Lee, Sol Kim, Soo An Shin, Sung Hoo Jhon, Yong Uk Shin
Принадлежит: CJ CHEILJEDANG CORP

The present invention provides methods for the production of cysteine or derivates thereof by culturing a microorganism having reduced activity of endogenous phosphoserine phosphatase and the activity of PhnC, PhnD, and PhnE is reduced, and enhanced activity of phosphoglycerate dehydrogenase and/or phosphoserine aminotransferase. The O-phosphoserine produced by such an organism can then be reacted with a sulfide in the presence of a sulfydrylase or a microorganism expressing a sulfhydrylase to produce cysteine or a derivative thereof. Microorganisms having these reduced and enhanced properties noted above are also provided herein.

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Номер записи: 5
26-07-2012 дата публикации

Aflatoxin production inhibitor and method for controlling aflatoxin contamination using the same

Номер: US20120190746A1
Автор: Ikuko Kurata, Keita Nakamura, Shohei Sakuda, Tetsuo Akiyama, Yasuhiko Muraoka, Yoshikazu Takahashi
Принадлежит: Microbial Chemistry Research Foundation, University of Tokyo NUC

The present invention relates to provide an aflatoxin production inhibitor that inhibits aflatoxin production specifically and efficiently, is highly safe, and is practical, and an efficient production method thereof; and a method for controlling aflatoxin contamination that uses the aflatoxin production inhibitor, specifically relating to an aflatoxin production inhibitor that includes at least one of a dioctatin represented by the following formula (I) and a derivative thereof, as an active ingredient: where, in the formula (I), R represents one of hydrogen and a methyl group.

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Номер записи: 6
04-10-2012 дата публикации

Use of inducible promoters in the production of methionine

Номер: US20120252077A1
Автор: Perrine Vasseur, Rainer Figge
Принадлежит: Metabolic Explorer SA

The present invention relates to use of inducible promoters in the production of methionine by fermentation. The present invention concerns a method for the production of methionine, its precursors or derivatives in a fermentative process comprising the following steps: culturing a modified microorganism in an appropriate culture medium comprising a source of carbon, a source of sulphur and a source of nitrogen, and recovering methionine and/or its derivatives from the culture medium, wherein in said modified microorganism, the expression of at least one gene involved in methionine production is under the control, direct or indirect, of a heterologous inducible promoter. The invention also concerned the modified microorganism used in the method.

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Номер записи: 7
01-11-2012 дата публикации

Method for producing an l-amino acid

Номер: US20120276598A1
Автор: Hisashi Yasueda, Ippei Inoue
Принадлежит: Individual

A method for efficiently producing an L-amino acid, especially L-lysine, by using a γ-proteobacterium is provided. In a method for producing an L-amino acid comprising culturing a bacterium belonging to γ-Proteobacteria and having an ability to produce an L-amino acid, for example, an Enterobacteriaceae bacterium such as Escherichia coli , in a medium containing glycerol as a carbon source to produce and accumulate the L-amino acid in the medium, and collecting the L-amino acid from the medium, a bacterium modified so that the activity of the Cnu protein is reduced is used as the bacterium.

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Номер записи: 8
29-11-2012 дата публикации

Process for preparing a carbamate compound

Номер: US20120302782A1
Автор: Mayumi Araki, Yasuhito Yamamoto, Yasutaka Yoshida
Принадлежит: UBE Industries Ltd

There is provided a process for preparing a carbamate compound, which is easy and commercially advantageous in that a carbamate compound can be produced with high yield from an amine compound and a carbonate compound. A process for preparing a carbamate compound which comprises the step of reacting an amine compound which has at least one amino group per molecule wherein the amine compound is selected from the group consisting of an aliphatic amine which may be substituted by an alicyclic group or an aromatic group or which may be interrupted by an alicyclic group or an aromatic group, and an alicyclic amine which may be substituted by an aliphatic group, with a carbonate compound in the presence of at least one organic solvent selected from the group consisting of a saturated cyclic hydrocarbon, an unsaturated cyclic hydrocarbon, and a non-cyclic ether by using a hydrolase.

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Номер записи: 9
07-03-2013 дата публикации

Novel amidase, gene for the same, vector, transformant, and method for production of optically active carboxylic acid amide and optically active carboxylic acid by using any one of those items

Номер: US20130059348A1
Автор: Daisuke Moriyama, Masutoshi Nojiri, Naoaki Taoka, Tozo Nishiyama
Принадлежит: Kaneka Corp

The present invention has its object to provide a novel polypeptide having amidase activity to selectively hydrolyze S-enantiomer in racemic nipecotamide, a DNA encoding the polypeptide, a vector containing the DNA, a transformant transformed with the vector, and a method for producing an optically active carboxylic acid amide and an optically active carboxylic acid in which a racemic carboxylic acid amide is hydrolyzed with the polypeptide or the transformant.

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Номер записи: 10
21-03-2013 дата публикации

ACYL AMINO ACIDS

Номер: US20130071885A1
Автор: Jarrell Kevin A., Reznik Gabriel, Vishwanath Prashanth
Принадлежит:

Engineered polypeptides useful in synthesizing acyl amino acids are provided. Also provided are methods of making acyl amino acids using engineered polypeptides. In certain embodiments, an acyl amino acid produced using compositions and/or methods of the present invention comprises cocoyl glutamate. 1. A method of producing an acyl amino acid , comprising steps of:providing an engineered polypeptide comprising a fatty acid linkage domain, a peptide synthetase domain, and a thioesterase domain;which fatty acid linkage domain, peptide synthetase domain and thioesterase domain are covalently linked;providing fatty acid recognized by the fatty acid linkage domain;providing an amino acid recognized by the peptide synthetase domain;incubating the engineered polypeptide, fatty acid, and amino acid under conditions and for a time sufficient for the fatty acid linkage domain to link the fatty acid to the amino acid to generate an acyl amino acid;incubating the engineered polypeptide and the acyl amino acid under conditions and for a time sufficient for the thioesterase domain to catalyze release of the acyl amino acid from the engineered polypeptide.2. A method of producing an acyl amino acid , comprising steps of:providing an engineered polypeptide comprising a fatty acid linkage domain, a peptide synthetase domain, and a reductase domain;which fatty acid linkage domain, peptide synthetase domain and reductase domain are covalently linked;providing a fatty acid recognized by the fatty acid linkage domain;providing an amino acid recognized by the peptide synthetase domain;incubating the engineered polypeptide, fatty acid, and amino acid under conditions and for a time sufficient for the fatty acid linkage domain to link the fatty acid to the amino acid to generate an acyl amino acid;incubating the engineered polypeptide and the acyl amino acid under conditions and for a time sufficient for the reductase domain to catalyze release of the acyl amino acid from the engineered ...

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Номер записи: 11
21-03-2013 дата публикации

Process for Producing Aliskiren

Номер: US20130071899A1
Автор: Adele Russo, Antonio Carlo Zanotti-Gerosa, Elena Cini, Luca Banfi, Luca Carcone, Marcello Rasparini, Maurizio Taddei, Renata Riva, Romina Vitale, Stephen Roseblade
Принадлежит: Chemo Iberica SA

A new route of synthesis of the compound Aliskiren of formula (I), used in the treatment of hypertension, is described.

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Номер записи: 12
28-03-2013 дата публикации

METHOD FOR PRODUCING AN L-AMINO ACID USING A BACTERIUM OF THE ENTEROBACTERIACEAE FAMILY HAVING ATTENUATED EXPRESSION OF GENES ENCODING A LYSINE/ARGININE/ ORNITHINE TRANSPORTER

Номер: US20130078681A1
Автор: Gusyatiner Mikhail Markovich, Rostova Yulia Georgievna, Voroshilova Elvira Borisovna
Принадлежит: AJINOMOTO CO., INC.

The present invention provides a method for producing an L-amino acid using a bacterium of the Enterobacteriaceae family, particularly a bacterium belonging to genus or in which expression of a gene encoding a lysine/arginine/ornithine transporter has been attenuated. 1. An L-amino acid-producing bacterium of the Enterobacteriaceae family , wherein said bacterium has been modified to attenuate expression of one or more genes encoding a lysine/arginine/ornithine transporter.2. The bacterium according to claim 1 , wherein said one or more genes encoding a lysine/arginine/ornithine transporter is/are one or more genes of argT-hisJQMP cluster.3. The bacterium according to claim 1 , wherein expression of said one or more genes encoding a lysine/arginine/ornithine transporter is/are attenuated by inactivation of said one or more genes.4. The bacterium according to claim 2 , wherein said one or more genes of the argT-hisJQMP cluster is/are inactivated.5Escherichia.. The bacterium according to claim 1 , wherein said bacterium belongs to genus6Escherichia coli.. The bacterium according to claim 5 , wherein said bacterium is7Pantoea.. The bacterium according to claim 1 , wherein said bacterium belongs to genus8. The L-amino acid-producing bacterium according to claim 1 , wherein said L-amino acid is a diaminomonocarboxylic acid.9. The L-amino acid-producing bacterium according to claim 8 , wherein said diaminomonocarboxylic acid is selected from the group consisting of L-lysine claim 8 , L-arginine claim 8 , L-ornithine claim 8 , and L-citrulline.10. A method for producing an L-amino acid comprising:{'claim-ref': {'@idref': 'CLM-00001', 'claim 1'}, 'cultivating the bacterium according to in a medium, and'}collecting said L-amino acid from the medium.11. The method according to claim 10 , wherein said L-amino acid is a diaminomonocarboxylic acid.12. The method according to claim 11 , wherein said diaminomonocarboxylic acid is selected from the group consisting of L-lysine ...

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Номер записи: 13
28-03-2013 дата публикации

Method for Producing an L-Amino Acid Using a Bacterium of the Enterobacteriaceae Family, Having Attenuated Expression of Gene(s) Encoding Peptidase

Номер: US20130078682A1
Автор: Filippov Dmitriy Vladimirovich, Gusyatiner Mikhail Markovich, Leonova Tatyana Viktorovna, Moriya Mika, Nagai Yuri, Noguchi Keiko, Voroshilova Elvira Borisovna
Принадлежит: AJINOMOTO CO., INC.

The present invention provides a method for producing L-amino acids, such as L-arginine, L-citrulline, and L-lysine, using a bacterium of the Enterobacteriaceae family, particularly a bacterium belonging to the genus or , which has been modified to attenuate expression of one or more genes, such as the pepA, pepB, and pepD genes. 1. A bacterium of the Enterobacteriaceae family having an ability to produce an L-amino acid , wherein said bacterium has been modified to attenuate expression of a gene selected from the group consisting of pepA , pepB , pepD , and combinations thereof.2. The bacterium according to claim 1 , wherein expression of the gene(s) is/are attenuated by inactivation of the gene(s).3Escherichia.. The bacterium according to claim 1 , wherein said bacterium belongs to the genus4Escherichia coli.. The bacterium according to claim 3 , wherein said bacterium is5Pantoea.. The bacterium according to claim 1 , wherein said bacterium belongs to the genus6. The bacterium according to claim 1 , wherein the L-amino acid is selected from the group consisting of L-arginine claim 1 , L-citrulline claim 1 , and L-lysine.7. The bacterium according to claim 1 , wherein the bacterium has been modified to attenuate expression of pepA claim 1 , pepB claim 1 , and pepD genes claim 1 , and the L-amino acid is L-lysine.8. A method for producing an L-amino acid comprising:{'claim-ref': {'@idref': 'CLM-00001', 'claim 1'}, 'cultivating the bacterium according to in a culture medium, and'}collecting the L-amino acid from the culture medium.9. The method according to claim 8 , wherein said L-amino acid is selected from the group consisting of L-arginine claim 8 , L-citrulline claim 8 , and L-lysine. This application is a Continuation of, and claims priority under 35 U.S.C. §120 to, International Application No. PCT/JP2011/063301, filed Jun. 3, 2011, and claims priority therethrough under 35 U.S.C. §119 to Russian Patent Application No. 2010122647, filed Jun. 3, 2010, the ...

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Номер записи: 14
28-03-2013 дата публикации

Host Cells and Methods for Producing Cinnamoyl Anthranilate and Analogs Thereof

Номер: US20130078683A1
Автор: Eudes Aymerick Guillaume, Loque Dominique
Принадлежит: The Regents of the University of California

The present invention provides for a method of producing a cinnamoyl anthranilate, or analog thereof, in a genetically modified host cell. 1. A genetically modified host cell comprising an hydroxycinnamoyl/benzoyl-CoA:anthranilate N-hydroxycinnamoyl/benzoyltransferase (HCBT , EC 2.3.1.144) , or functional fragment thereof , capable of catalyzing the formation of a cinnamoyl anthranilate , or analog thereof , from a cinnamoyl-CoA , or analog thereof , and an anthranilate , or analog thereof.2Dianthus caryophyllus. The host cell of claim 1 , wherein the HCBT has an amino acid sequence at least 70% identical to the amino acid sequence of HCBT.3Dianthus caryophyllus. The host cell of claim 2 , wherein the HCBT is a HCBT.4. The host cell of further comprising a 4-coumarate:CoA ligase (4CL claim 1 , EC 6.2.1.12) claim 1 , or functional fragment thereof claim 1 , capable of catalyzing the formation of a cinnamic acid claim 1 , or analog thereof claim 1 , into a corresponding cinnamoyl-CoA thioester claim 1 , or analog thereof.5Arabidopsis thaliana.. The host cell of claim 1 , wherein the 4CL has an amino acid sequence at least 70% identical to the amino acid sequence of 4-coumarate:CoA ligase 5 (4CL5) of6Arabidopsis thaliana.. The host cell of claim 5 , wherein the 4CL is a 4-coumarate:CoA ligase 5 (4CL5) of7. The host cell of claim 4 , wherein the cinnamic acid claim 4 , or analog thereof claim 4 , is a hydroxycinnamic acid claim 4 , and the host cell lacks any enzyme capable of catalyzing the decarboxylation of a hydroxycinnamic acid.8. The host cell of claim 7 , wherein the host cell is a yeast cell and the pad1 gene is deleted or has a reduction of expression claim 7 , or the host cell has a reduced capability to catabolize claim 7 , metabolize claim 7 , or modify the hydroxycinnamic acid claim 7 , or analog thereof.10. A method of producing a cinnamoyl anthranilate claim 1 , or analog thereof claim 1 , comprising: culturing the genetically modified host cell of under ...

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Номер записи: 15
28-03-2013 дата публикации

METHOD FOR PRODUCING 1,5-PENTAMETHYLENEDIAMINE, 1,5-PENTAMETHYLENEDIAMINE, 1,5-PENTAMETHYLENE DIISOCYANATE, METHOD FOR PRODUCING 1,5-PENTAMETHYLENE DIISOCYANATE, POLYISOCYANATE COMPOSITION, AND POLYURETHANE RESIN

Номер: US20130079486A1
Автор: HASEGAWA Daisuke, Hidesaki Tomonori, KUWAMURA Goro, NAKAGAWA Toshihiko, Natsuji Akiko, Sato Kuniaki, TAKEUCHI Hiroshi, Yamasaki Satoshi
Принадлежит:

In a method for producing 1,5-pentamethylenediamine, a lysine decarboxylase-expressing microorganism that is subjected to a treatment is used. 1. A method for producing 1 ,5-pentamethylenediamine , using a lysine decarboxylase-expressing microorganism that is subjected to a treatment.2. The method for producing 1 claim 1 ,5-pentamethylenediamine according to claim 1 , wherein the treatment is at least one or more of a freeze-thaw treatment claim 1 , a heat treatment claim 1 , and a lysine salt treatment.3. The method for producing 1 claim 2 ,5-pentamethylenediamine according to claim 2 , wherein the freezing temperature in the freeze-thaw treatment is −80° C. or more and a solidification point or less of the lysine decarboxylase-expressing microorganism or its suspension.4. The method for producing 1 claim 2 ,5-pentamethylenediamine according to claim 2 , wherein the dry bacterial cell-based concentration in the freeze-thaw treatment is 3 mass % or more and 25 mass % or less.5. The method for producing 1 claim 2 ,5-pentamethylenediamine according to claim 2 ,wherein in the freeze-thaw treatment, the freezing temperature is more than −80° C., and/or the dry bacterial cell-based concentration is below 25 mass %.6. The method for producing 1 claim 2 ,5-pentamethylenediamine according to claim 2 ,wherein in the freeze-thaw treatment, the freezing temperature and the dry bacterial cell-based concentration satisfy the following condition of (a) or (b):(a) a freezing temperature of −80° C. or less and a dry bacterial cell-based concentration of 3 mass % or more and 15 mass % or less; or(b) a freezing temperature of −10° C. or less and −30° C. or more and a dry bacterial cell-based concentration of 3 mass % or more and 25 mass % or less.7. The method for producing 1 claim 2 ,5-pentamethylenediamine according to claim 2 , wherein the heat treatment temperature is 50° C. or more and below 70° C.8. The method for producing 1 claim 2 ,5-pentamethylenediamine according to claim ...

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Номер записи: 16
04-04-2013 дата публикации

Method for Producing an L-Amino Acid

Номер: US20130084609A1
Автор: Hashiro Shuhei, SUZUKI Shigeo, Usuda Yoshihiro
Принадлежит: AJINOMOTO CO., INC.

An L-amino acid is produced by culturing a bacterium having an L-amino acid-producing ability in a medium containing a processed product of a microalga which promotes production and accumulation of the L-amino acid by the bacterium. The process product is produced by disrupting the culture of the microalga, and/or extracting the culture of the microalga, or fractionating the culture of the microalga or the disrupted culture. The processed product contains a mixture of organic substances produced by the microalga, a hydrolysate of the disrupted microalga culture, and/or an extract or fractionation product of the microalga culture. The processed product can also contain a saccarification product of starch or a hydrolysate of fats and oils. The bacterium is cultured to produce and accumulate the L-amino acid in culture, and the L-amino acid is collected from the culture. 2. The method according to claim 1 , wherein the processed product is selected from the group consisting of:(1) a disruption product of a culture of the microalga,(2) an extract or a fractionation product of a disruption product of a culture of the microalga comprising a mixture of organic substances,(3) a hydrolysate of a disruption product of a culture of the microalga,(4) a hydrolysate of an extract or a fractionation product of a disruption product of a culture of the microalga comprising a mixture of organic substances, and(5) combinations thereof.3. The method according to claim 1 , wherein the processed product is selected from the group consisting of:(1) a saccharification product of a disruption product of alga bodies of the microalga,(2) a saccharification product of an extract or a fractionation product of a disruption product of alga bodies of the microalga, wherein the extract or fractionation product comprises starch, and(3) combinations thereof.4. The method according to claim 3 , wherein the saccharification product is obtained from the reaction of a disruption product of alga bodies of ...

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Номер записи: 17
11-04-2013 дата публикации

BIOCATALYSTS AND METHODS FOR THE SYNTHESIS OF (S)-3-(1-AMINOETHYL)-PHENOL

Номер: US20130089898A1
Автор: Cabirol Fabien, Gohel Anupam, Lalonde James, Oh Seong Ho, SMITH Derek, Wong Brian
Принадлежит: CODEXIS, INC.

The present disclosure provides engineered transaminase polypeptides having improved properties as compared to naturally occurring transaminases including the ability of converting the substrate, 3′-hydroxyacetophenone to (S)-3-(1-aminoethyl)-phenol in enantiomeric excess and high percentage conversion. Also provided are polynucleotides encoding the engineered transaminases, host cells capable of expressing the engineered transaminases, and methods of using the engineered transaminases to synthesize (S)-3-(1-aminoethyl)-phenol and related compounds useful in the production of active pharmaceutical ingredients. 2. The polypeptide of in which the transaminase polypeptide has at least 1.2 times the activity of SEQ ID NO:2 in the rate of conversion of 3-hydroxyacetophenone to (S)-3-(1-aminoethyl)-phenol under reaction conditions of 35 g/L of 3-hydroxyacetophenone claim 1 , 1.5 M isopropylamine claim 1 , 1 mM pyridoxal phosphate claim 1 , 5% v/v DMSO claim 1 , pH 7.5 claim 1 , and 45° C.3. The polypeptide of in which the amino acid residue differences as compared to SEQ ID NO: 2 are selected from the following:residue at position X18 is A;residue at position X163 is F or H;residue at position X235 is P;residue at position X244 is T;residue at position X323 is T;residue at position X383 is V;residue at position X424 is A; andresidue at position X427 is Y.4. The polypeptide of or in which the transaminase polypeptide amino acid sequence has additional amino acid residue differences as compared to SEQ ID NO:2 at one or more of the following positions: X21 claim 1 , X31 claim 1 , X74; X113 claim 1 , X122 claim 1 , X130 claim 1 , X133 claim 1 , X146 claim 1 , X147 claim 1 , X153 claim 1 , X164 claim 1 , X167 claim 1 , X168 claim 1 , X174 claim 1 , X233 claim 1 , X245 claim 1 , X286 claim 1 , X293 claim 1 , X315 claim 1 , X316 claim 1 , X318 claim 1 , X332 claim 1 , X375 claim 1 , X394 claim 1 , and X418.5. The polypeptide of in which the additional amino acid residue ...

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Номер записи: 18
18-04-2013 дата публикации

PROCESS FOR PRODUCTION OF CADAVERINE

Номер: US20130095534A1
Автор: Mimitsuka Takashi, Sawai Hideki, Suda Kazumi
Принадлежит: TORAY INDUSTRIES INC

By a method for producing cadaverine by culturing a microorganism that extracellularly secretes lysine decarboxylase, by-production of lysine is suppressed, the yield of cadaverine relative to glucose consumption is improved compared to conventional production methods, and further, the load on the purification step in purification of cadaverine as a raw material for polyamide can be reduced. 1. A method for producing cadaverine comprising culturing a microorganism that extracellularly secretes lysine decarboxylase.2. The method according to claim 1 , wherein lysine is added to a medium to culture said microorganism.3. The method according to claim 1 , wherein said microorganism intracellularly expresses a protein comprising lysine decarboxylase having a secretory signal peptide attached to the N-terminus side of the amino acid sequence thereof claim 1 , which lysine decarboxylase is thereby extracellularly secreted.4. The method according to claim 3 , wherein said microorganism has a gene construct comprising claim 3 , in a direction from 5′ to 3′ of the nucleic acid sequence claim 3 , a promoter sequence that functions in the microorganism claim 3 , a nucleic acid sequence encoding said secretory signal peptide and a nucleic acid sequence encoding lysine decarboxylase claim 3 , which gene construct allows intracellular expression of said protein comprising lysine decarboxylase having said secretory signal peptide attached to the N-terminus side of the amino acid sequence thereof.5. The method according to claim 3 , wherein said secretory signal peptide is a peptide represented by the amino acid sequence shown in any of SEQ ID NOs: 13 to 43.6E. coli.. The method according to claim 1 , wherein said lysine decarboxylase is derived from7E. coli.. The method according to claim 1 , wherein said microorganism is a coryneform bacterium or8. The method according to claim 2 , wherein said microorganism intracellularly expresses a protein comprising lysine decarboxylase ...

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Номер записи: 19
18-04-2013 дата публикации

ENZYMATIC RESOLUTION OF RACEMIC (2R,S)-2-(ACETYLAMINO)-3-METHOXY-N-(PHENYLMETHYL)PROPANAMIDE

Номер: US20130095535A1
Автор: Bosch i Lladó Jordi, Duran Lopez Ernesto
Принадлежит: MEDICHEM, S.A.

The present invention is concerned with a process of preparing (R)-lacosamide. The process comprises providing an (R,S)-lacosamide precursor and contacting the same with at least an enzyme in the presence of a solvent. The enzyme either stereoselectively hydrolyzes or acetylates an (R)- or (S)-enantiomer of the (R,S)-lacosamide precursor. The process further comprises where appropriate also concurrently, or successively, employing one or more reagents capable of converting the hydrolysed or acetylated (R)- or (S)-enantiomer to (R)-lacosamide. 140.-. (canceled)42. The process of claim 41 , wherein step (ii) comprises contacting the (R claim 41 ,S)-compound of formula (II) with one or more enzymes in the presence of a solvent and optionally an acetyl donor compound to form an enantiomerically enriched or enantiomerically pure (R)-enantiomer of the compound formula (II) wherein Ris CHC(═O)— claim 41 ,{'sub': '1', 'wherein the one or more enzymes is capable of stereoselectively hydrolyzing the (R)- or (S)-enantiomer of a compound of formula (II) when the solvent is a protic solvent or is capable of stereoselectively acetylating the (R)-enantiomer of a compound of formula (II) when Ris a first intermediate moiety and when an acetyl donor compound is present, and'}{'sub': '2', 'wherein step (iii) comprises optionally further comprising contacting the (R,S)-compound of formula (II) or the enriched or enantiomerically pure (R)-enantiomer of the compound formula (II) with one or more reagents capable of converting a second intermediate moiety into —NHCHPh.'}45. The process of claim 41 , wherein the enzyme capable of stereoselectively acetylating either the (R)- or (S)-enantiomer of a compound of formula (II) is a lipase.46Candida antarcticaCandida antarcticaPseudomonas cepacia. The process of claim 45 , wherein the lipase is selected from the group consisting of lipase A (CAL-A) claim 45 , lipase B (CAL-B) claim 45 , and lipase.47. The process of claim 43 , wherein the ...

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Номер записи: 20
25-04-2013 дата публикации

Microorganism with Enhanced L-Lysine Productivity and Method for Producing L-Lysine Using the Same

Номер: US20130102037A1
Автор: Hyung Joon Kim, Jae Woo Jang, Jae Yong Cho, Jun Ok Moon, Sang Jo Lim
Принадлежит: CJ CHEILJEDANG CORP

Disclosed is an L-lysine-producing microorganism having gluconate kinase activity weakened in comparison to the endogenous activity thereof, and methods provided for preparing the microorganism and for producing L-lysine using the same.

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Номер записи: 21
16-05-2013 дата публикации

PROCESS FOR PRODUCING SULFUR-CONTAINING alpha- AMINO ACID COMPOUND

Номер: US20130122556A1
Автор: Asako Hiroyuki
Принадлежит: Sumitomo Chemical Company, Limited

The present invention provides a novel process for producing a sulfur-containing α-amino acid compounds such as methionine. A process for producing a sulfur-containing α-amino acid compound (Compound 2) comprising a step of reacting a specific sulfur-containing amino alcohol compound (Compound 1) with the following transformants and others: (a) both a transformant in which has been introduced into a microorganism cell a gene of an enzyme capable of converting the Compound 1 into a corresponding sulfur-containing α-amino aldehyde compound (Compound 3) (Capability A) and a transformant in which has been introduced into a microorganism cell a gene of an enzyme capable of converting the Compound 3 into a corresponding Compound 2, (b) a transformant in which has been introduced into a microorganism cell both a gene of an enzyme which has Capability A and a gene of an enzyme which has Capability B, or (c) a transformant in which has been introduced into a microorganism cell a gene of an enzyme which has both Capability A and Capability B. 2. The process according to wherein the transformant is the transformant in which has been introduced into a microorganism cell a polynucleotide comprising a nucleotide sequence encoding an amino acid sequence of an enzyme that is capable of converting the above sulfur-containing amino alcohol compound into a corresponding sulfur-containing α-amino aldehyde compound as well as capable of converting the above sulfur-containing α-amino aldehyde compound into a corresponding sulfur-containing α-amino acid compound claim 1 , wherein said enzyme comprises any of the following amino acid sequences:a) the amino acid sequence of SEQ ID NO: 1,b) an amino acid sequence which is encoded by a nucleotide sequence of a DNA that hybridizes to a DNA consisting of the nucleotide sequence of SEQ ID NO: 2 or 5 under a stringent condition and which is an amino acid sequence of an enzyme that is capable of converting the above sulfur- ...

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Номер записи: 22
30-05-2013 дата публикации

PROCESS FOR PRODUCING SULFUR-CONTAINING ALPHA-AMINO ACID COMPOUND

Номер: US20130137148A1
Автор: Asako Hiroyuki
Принадлежит: Sumitomo Chemical Company, Limited

The present invention provides a novel process for producing a sulfur-containing α-amino acid compound such as methionine. A process for producing a sulfur-containing α-amino acid compound represented by the formula (2): wherein Rrepresents hydrogen, an alkyl group having 1 to 8 carbon atoms, or an aryl group having 6 to 20 carbon atoms; comprising a step of reacting a sulfur-containing amino alcohol compound represented by the formula (1): wherein Ris the same as defined above, with a microbial cell or a processed product of the microbial cell of a microorganism capable of converting the sulfur-containing amino alcohol compound into a corresponding sulfur-containing α-amino acid compound. 2. The process according to wherein the microorganism is capable of preferentially oxidizing the hydroxyl group of the sulfur-containing amino alcohol compound.3AlcaligenesBacillusPseudomonasRhodobacterRhodococcus.. The process according to wherein the microorganism is one or more microorganisms selected from a group consisting of microorganisms of the genus claim 1 , microorganisms of the genus claim 1 , microorganisms of the genus claim 1 , microorganisms of the genus and microorganisms of the genus4Alcaligenes denitrificans, Alcaligenes eutrophus, Alcaligenes faecalis, AlcaligenesAlcaligenes xylosoxydans, Bacillus alvei, Bacillus badius, Bacillus brevis, Bacillus cereus, Bacillus coagulans, Bacillus firmus, Bacillus licheniformis, Bacillus moritai, Bacillus pumilus, Bacillus sphaericus, Bacillus subtilis, Bacillus validus, Pseudomonas denitrificans, Pseudomonas ficuserectae, Pseudomonas fragi, Pseudomonas mendocina, Pseudomonas oleovorans, Pseudomonas ovalis, Pseudomonas pseudoalcaligenes, Pseudomonas putida, Pseudomonas putrefaciens, Pseudomonas riboflavina, Pseudomonas straminea, Pseudomonas syringae, Pseudomonas tabaci, Pseudomonas taetrolens, Pseudomonas vesicularis, Rhodobacter sphaeroides, Rhodococcus erythropolis, Rhodococcus groberulus, Rhodococcus ...

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Номер записи: 23
20-06-2013 дата публикации

PROCESS FOR PRODUCING SULFUR-CONTAINING ALPHA-AMINO ACID COMPOUND

Номер: US20130157320A1
Автор: Asako Hiroyuki
Принадлежит: Sumitomo Chemical Company, Limited

The present invention provides a novel process for producing a sulfur-containing α-amino acid compound such as methionine. A process for producing a sulfur-containing α-amino acid compound represented by the formula (2): wherein Rrepresents hydrogen, an alkyl group having 1 to 8 carbon atoms, or an aryl group having 6 to 20 carbon atoms; comprising: a first step of culturing a microorganism capable of converting a sulfur-containing amino alcohol compound represented by the formula (1): wherein Ris the same as defined above into the corresponding sulfur-containing α-amino acid compound in a culture medium containing a lower aliphatic alcohol to prepare a microbial cell of the microorganism; and a second step of reacting the sulfur-containing amino alcohol compound with the microbial cell of the microorganism obtained in the first step or a processed product of the microbial cell. 2. The process according to wherein the microorganism is capable of preferentially oxidizing the hydroxyl group of the sulfur-containing amino alcohol compound.3AlcaligenesBacillusPseudomonasRhodobacterRhodococcus.. The process according to wherein the microorganism is one or more microorganisms selected from a group consisting of microorganisms of the genus claim 1 , microorganisms of the genus claim 1 , microorganisms of the genus claim 1 , microorganisms of the genus and microorganisms of the genus4Alcaligenes denitrificans, Alcaligenes eutrophus, Alcaligenes faecalis, AlcaligenesAlcaligenes xylosoxydans, Bacillus alvei, Bacillus badius, Bacillus brevis, Bacillus cereus, Bacillus coagulans, Bacillus firmus, Bacillus licheniformis, Bacillus moritai, Bacillus pumilus, Bacillus sphaericus, Bacillus subtilis, Bacillus validus, Pseudomonas denitrificans, Pseudomonas ficuserectae, Pseudomonas fragi, Pseudomonas mendocina, Pseudomonas oleovorans, Pseudomonas ovalis, Pseudomonas pseudoalcaligenes, Pseudomonas putida, Pseudomonas putrefaciens, Pseudomonas riboflavina, Pseudomonas straminea, ...

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Номер записи: 24
20-06-2013 дата публикации

Use of Phosphoketolase for Producing Useful Metabolites

Номер: US20130157321A1
Автор: Chinen Akito, Hara Yoshihiko, Izui Hiroshi, Katashkina Joanna Yosifovna, Kozlov Yury Ivanovich, Rybak Konstantin Vyacheslavovich, Slivinskaya Ekaterina Aleksandrovna, Yasueda Hisashi
Принадлежит: AJINOMOTO CO., INC.

The present invention provides a bacterium which has an ability to produce a useful metabolite derived from acetyl-coenzyme A, such as L-glutamic acid, L-glutamine, L-proline, L-arginine, L-leucine, L-cysteine, succinate, and polyhydroxybutyrate, wherein said bacterium is modified so that activities of D-xylulose-5-phosphate phosphoketolase and/or fructose-6-phosphate phosphoketolase are enhanced. The present invention also provides a method for producing the useful metabolite using the bacterium. 1. A method for producing a useful metabolite derived from acetyl-coenzyme A comprising cultivating a bacterium in a culture medium to produce a useful metabolite derived from acetyl-coenzyme A in the culture medium and/or the bacterium , and collecting said useful metabolite from the culture medium and/or the bacterium , wherein said bacterium is modified to have an increased activity of D-xylulose-5-phosphate phosphoketolase and/or fructose-6-phosphate phosphoketolase.2. The method according to claim 1 , wherein the useful metabolite is selected from the group consisting of L-glutamic acid claim 1 , L-glutamine claim 1 , L-proline claim 1 , L-arginine claim 1 , L-leucine claim 1 , L-cysteine claim 1 , succinate claim 1 , and polyhydroxybutyrate.3. The method according to claim 1 , wherein the bacterium inherently does not have an activity of D-xylulose-5-phosphate phosphoketolase and fructose-6-phosphate phosphoketolase claim 1 , and wherein said bacterium is transformed with a DNA fragment coding for D-xylulose-5-phosphate phosphoketolase and/or fructose-6-phosphate phosphoketolase.4. The method according to claim 1 , wherein the bacterium is further modified to have a reduced activity of 6-phosphofructokinase.5Bacillus. The method according to claim 1 , wherein the bacterium is selected from the group consisting of Enterobacteriaceae claim 1 , coryneform bacterium claim 1 , and bacterium.6EscherichiaPantoea.. The method according to claim 1 , wherein the bacterium ...

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Номер записи: 25
20-06-2013 дата публикации

MUTANT MICROORGANISM HAVING HIGH PRODUCTION OF CADAVERINE, AND PREPARATION METHOD OF CADAVERINE USING SAME

Номер: US20130157323A1
Автор: KIM Min Young, LEE Sang Yup, Qian Zhi Gang, Xia Xiaoxia
Принадлежит: KOREA ADVANCED INSTITUTE OF SCIENCE AND TECHNOLOGY

The present invention relates to a mutant microorganism having a high ability to produce cadaverine, and a method for producing cadaverine using the same. More specifically, the invention relates to a mutant microorganism having a high ability to produce cadaverine wherein a gene involved in the cadaverine degradation or utilization pathway is inactivated or deleted, and to a method for producing cadaverine in high yield by culturing the mutant microorganism under aerobic conditions. The mutant microorganism according to the present invention is useful for producing a high yield of cadaverine which can be widely used in various industrial applications. 1. A mutant microorganism having the ability to produce cadaverine wherein at least one gene selected from the group consisting of a speE gene encoding putrescine/cadaverine aminopropyl transferase , a speG gene encoding spermidine N-acetyltransferase , a ygjG gene encoding putrescine/cadaverine aminotransferase , a puuP gene encoding putrescine importer , and a puuA gene encoding glutamate-putrescine/glutamate-cadaverine ligase , which are involved in the cadaverine degradation or utilization pathway , is inactivated or deleted.2. The mutant microorganism of claim 1 , wherein a lacI gene encoding a lac operon repressor is further deleted in order to increase the expression of genes encoding enzymes which are involved in cadaverine biosynthesis.3. The mutant microorganism of claim 1 , wherein a cadA gene encoding lysine decarboxylase is further introduced or amplified.4. The mutant microorganism of claim 3 , wherein the cadA gene encoding lysine decarboxylase is introduced in the form of an expression vector containing a strong promoter.5. The mutant microorganism of claim 4 , wherein the strong promoter is selected from the group consisting of a trc promoter claim 4 , a tac promoter claim 4 , a T7 promoter claim 4 , a lac promoter claim 4 , and a trp promoter. ...

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Номер записи: 26
04-07-2013 дата публикации

L-Amino Acid-Producing Bacterium and Method for Producing L-Amino Acid

Номер: US20130171700A1
Автор: Gunji Yoshiya, Miyata Yuri, Oba Manami, Shimaoka Megumi, Sugimoto Shinichi, Tsujimoto Nobuharu, Yasueda Hisashi
Принадлежит: AJINOMOTO CO., INC.

An L-amino acid is produced by culturing a bacterium which can grow by using methanol as the main carbon source and has L-amino acid-producing ability, for example, a bacterium in which dihydrodipicolinate synthase activity and aspartokinase activity are enhanced by transformation of cells with a DNA coding for dihydrodipicolinate synthase that is desensitized to feedback inhibition by L-lysine and a DNA coding for aspartokinase that is desensitized to feedback inhibition by L-lysine, or a bacterium which is casamino acid auxotrophic, in a medium containing methanol as a main carbon source, to produce and accumulate an L-amino acid in culture, and collecting the L-amino acid from the culture. 1MethylophilusMethylophilusEscherichia coliEscherichia coli. A method for producing L-lysine comprising culturing a bacterium in a medium containing methanol to produce and accumulate L-lysine in the medium , and collecting L-lysine from the medium , wherein said bacterium has been modified to have enhanced activities of dihydrodipicolinate synthase and aspartokinase by transformation with a DNA from that encodes dihydrodipicolinate synthase resistant to feedback inhibition by L-lysine and with a DNA from that encodes aspartokinase resistant to feedback inhibition by L-lysine.2Escherichia coli. The method according to claim 1 , wherein said DNA from that encodes dihydrodipicolinate synthase encodes dihydrodipicolinate synthase comprising replacement of histidine at position 118 in SEQ ID NO: 2 with tyrosine.3Escherichia coli. The method according to claim 1 , wherein said DNA from that encodes aspartokinase encodes aspartokinase comprising replacement of threonine at position 352 in SEQ ID NO: 4 with isoleucine. This application is a Continuation of, and claims priority under 35 U.S.C. §120 to, U.S. patent application Ser. No. 11/738,617, filed Apr. 23, 2007, which was a Divisional of, and claims priority under U.S.C. §120 to, U.S. patent application Ser. No. 09/926,299, filed ...

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Номер записи: 27
18-07-2013 дата публикации

CANDIDA TROPICALIS CELLS AND USE THEREOF

Номер: US20130183725A1
Автор: Haas Thomas, Hennemann Hans-Georg, Poetter Markus, Schaffer Steffen
Принадлежит:

The invention relates to genetically engineered cells, use thereof and a method of production of ω-hydroxycarboxylic acids and ω-hydroxycarboxylic acid esters. 112-. (canceled)13. A method for production of ω-aminocarboxylic acids or ω-aminocarboxylic acid esters , comprising{'i': 'Candida tropicalis', 'a) contacting a cell with a medium comprising a carboxylic acid or a carboxylic acid ester,'}{'i': Candida tropicalis', 'Candida tropicalis, 'b) cultivating the cell under conditions that enable the cell to form corresponding ω-hydroxycarboxylic acid or ω-hydroxycarboxylic acid esters from the carboxylic acid or the carboxylic acid ester,'} {'i': 'Candida tropicalis', 'wherein the cell has, compared with its wild type, a reduced activity of at least one of enzyme encoded by an intron-free nucleic acid sequences selected from the group consisting of SEQ ID NO: 57 and a sequence that is 95% identical to SEQ ID NO: 57.'}, 'c) optionally isolating the ω-hydroxycarboxylic acid or ω-hydroxycarboxylic acid esters that formed, converting the ω-hydroxycarboxylic acids or corresponding esters into the ω-oxo-carboxylic acids or the corresponding esters and then aminating the oxo-group,'}14Candida tropicalisCandida tropicalisCandida tropicalisCandida tropicalisCandida tropicalis. The method according to claim 13 , wherein the reduced enzymatic activity comprises insertion of a foreign DNA into SEQ ID NO:57 contained in a chromosome of the cell claim 13 , deletion of at least a part of SEQ ID NO:57 in a chromosome of the cell claim 13 , a point mutation in SEQ ID NO:57 in a chromosome of the cell claim 13 , providing an interfering RNA molecule targeting expression of SEQ ID NO:57 claim 13 , and exchanging a part of SEQ ID NO:57 in a chromosome of the cell with foreign DNA claim 13 , and exchanging a part of a transcription promoter controlling expression of SEQ ID NO:57 in the cell with foreign DNA.15. The method according to claim 14 , wherein the foreign DNA is a selection ...

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Номер записи: 28
18-07-2013 дата публикации

METHODS FOR PRODUCING METHIONINE BY CULTURING A MICROORGANISM MODIFIED TO ENHANCE PRODUCTION OF CYSTEINE

Номер: US20130183726A1
Автор: Chateau Michel, Figge Rainer, Lux Fabien, Raynaud Céline, Soucaille Philippe
Принадлежит: METABOLIC EXPLORER

A method of producing methionine, derivatives or precursors thereof includes culturing a modified microorganism in a culture medium comprising a source of carbon and a source of sulfur; and recovering methionine from the culture medium, wherein said modified microorganism has an increased expression of cysE gene encoding serine acetyltransferase, metH gene encoding methionine synthase and metF gene encoding 5,10-methylenetetrahydrofolate reductase compared to expression of the cysE, metH and metF genes in an unmodified microorganism. 1. A method of producing methionine , derivatives or precursors thereof comprising:culturing a modified microorganism in a culture medium comprising a source of carbon and a source of sulfur; andrecovering methionine from the culture medium,wherein said modified microorganism has an increased expression of cysE gene encoding serine acetyltransferase, metH gene encoding methionine synthase and metF gene encoding 5,10-methylenetetrahydrofolate reductase compared to expression of the cysE, metH and metF genes in an unmodified microorganism.2. The method of claim 1 , wherein at least one other gene involved in cysteine production is overexpressed compared to the expression in an unmodified microorganism claim 1 , wherein said gene being selected from the group consisting ofcysA sulfate permease,cysU, cysT component of sulfate ABC transporter,cysW membrane bound sulfate transport protein,cysH adenylylsulfate reductase,cysI sulfite reductase, alpha subunit,cysJ sulfite reductase, beta subunit,cysM O-acetyl-sulfhydrylase,cysZ sulfate transport, andsbp Periplasmic sulfate-binding protein.3. The method of claim 1 , wherein at least one other gene involved in production of C1 units and/or transfer potential onto homocysteine is overexpressed compared to the expression in an unmodified microorganism claim 1 , wherein said gene being selected from the group consisting ofmetE encoding methionine synthase,glyA encoding serine hydroxymethyltransferase ...

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Номер записи: 29
18-07-2013 дата публикации

INCREASING NADPH AVAILABILITY FOR METHIONINE PRODUCTION

Номер: US20130183727A1
Автор: Boisart Cedric, Dischert Wanda, Figge Rainer, Vasseur Perrine
Принадлежит: METABOLIC EXPLORER

The present invention is related to a microorganism for the production of methionine, wherein said microorganism is modified to enhance the transhydrogenase activity of PntAB. In a preferred aspect of the invention, the activity of the transhydrogenase UdhA is attenuated in said microorganisms. The invention also related to a method for producing methionine by fermentation. 1. A microorganism for producing methionine , wherein said microorganism is modified to enhance transhydrogenase activity of PntAB.2. The microorganism of claim 1 , wherein genes encoding PntAB are overexpressed.3. The microorganism of claim 1 , wherein said microorganism is modified to attenuate activity of transhydrogenase UdhA.4. The microorganism of claim 3 , wherein the gene encoding UdhA is deleted.5. The microorganism of claim 1 , wherein said microorganism is modified to increase one carbon metabolism.6. The microorganism of claim 5 , wherein at least one of the following activities are enhanced:a. activity of methylenetetrahydrofolate reductase, MetF.b. activity of glycine cleavage complex, GcvTHP and Lpdc. activity of serine hydroxymethyltransferase, GlyAd. activity of methyltransferase, MetH or MetE.7. The microorganism of claim 6 , wherein said activity of MetF is enhanced by overexpressing the metF gene and/or by optimizing translation thereof.8. The microorganism of claim 7 , wherein said metF gene is under control of a strong promoter comprising at least one Ptrc family promoter.9. The microorganism of claim 1 , wherein expression of at least one of the following genes is increased: cysP claim 1 , cysU claim 1 , cysW claim 1 , cysA claim 1 , cysM claim 1 , cysI claim 1 , cysJ claim 1 , cysH claim 1 , cysE claim 1 , serA claim 1 , serB claim 1 , serC claim 1 , metA allele with reduced feed-back sensitivity claim 1 , thrA or thrA allele with reduced feed-back sensitivity.10. The microorganism of claim 9 , wherein at least one of said genes is under control of an inducible promoter.11 ...

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Номер записи: 30
01-08-2013 дата публикации

Process for the Production of Fine Chemicals

Номер: US20130198911A1
Автор: Blau Astrid, Chardonnens Agnes, Chen Ruoying, Kamlage Beate, Looser Ralf, McKersie Bryan, Plesch Gunnar, Puzio Piotr, Sarria-Millan Rodrigo, Shirley Amber, Wang Xi-Qing, Wendel Birgit
Принадлежит: BASF Plant Science GmbH

The present invention relates to a process for the production of fine chemicals in a microorganism, a plant cell, a plant, a plant tissue or parts thereof. The invention furthermore relates to nucleic acid molecules, polypeptides, nucleic acid constructs, vectors, antisense molecules, antibodies, host cells, plant tissue, propagation material, harvested material, plants, microorganisms as well as agricultural compositions and to their use. 1. A process for the production of a fine chemical , comprising increasing or generating in an organism or part thereof expression of at least one nucleic acid molecule selected from the group consisting of:a) a nucleic acid molecule encoding a polypeptide comprising the amino acid sequence of SEQ ID NO: 2, 4, 6, 8, 10, 12, 14, 16, 18, 20, 22, 24, 26, 28, 30, 32, 34, 36, 38, 40, 42, 44, 46, 56, 58, 60, 62, 64, 66, 68, 70, 72, 74, 76, 78, 80, 82, 84, 86, 88, 90, 92, 94, 96, 98, 100, 102, 104, 106, 108, 110, 112, 114, 116, 118, 120, 122, 124, 126, 128, 130, 132, 134, 136, 138, 140, 142, 144, 146, 148, 150, 152, 154, 156, 158, 160, 162, 164, 166, 168, 170, 172, 174, 176, 178, 180, 182, 184, 186, 188, 190, 192, 194, 196, 198, 200, 202, 204, 206, 208, 210, 212, 214, 216, 218, 220, 222, 224, 226, 228, 230, 232, 234, 236, 238, 240, 242, 244, 246, 248, 250, 252, 254, 256, 258, 260, 262, 264, 266, 268, 270, 272, 274, 276, 278, 280, 282, 284, 286, 288, 290, 292, 294, 296, 298, 300, 302, 304, 306, 308, 310, 312, 314, 316, 318, 320, 322, 324, 326, 328, 330, 332, 334, 336, 338, 340, 342, 344, 346, 348, 350, 352, 354, 356, 358, 360, 362, 364, 366, 368, 370, 372, 374, 376, 378, 380, 382, 384, 386, 388, 390, 392 or 394;b) a nucleic acid molecule comprising the nucleotide sequence of SEQ ID NO: 1, 3, 5, 7, 9, 11, 13, 15, 17, 19, 21, 23, 25, 27, 29, 31, 33, 35, 37, 39, 41 43, 45, 55, 57, 59, 61, 63, 65, 67, 69, 71, 73, 75, 77, 79, 81, 83, 85, 87, 89, 91, 93, 95, 97, 99, 101, 103, 105, 107, 109, 111, 113, 115, 117, 119, 121, 123, 125, 127, 129, 131, ...

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Номер записи: 31
08-08-2013 дата публикации

PRODUCTION PROCESS FOR AMINO ACIDS OF THE ASPARTATE FAMILY USING MICROORGANISMS

Номер: US20130203130A1
Автор: Becker Judith, Wittmann Christoph
Принадлежит: PAIK KWANG INDUSTRIAL CO., LTD.

The present invention is directed to a method utilizing a recombinant microorganism for the production of aspartate derived amino acids and precursors thereof, in particular for the production of L-lysine. Furthermore, the present invention relates to a recombinant microorganism having improved aspartate-derived amino acid synthesis activity in comparison to the initial microorganism and the use of such microorganisms in producing said amino acids and precursors and derivatives, in particular in the synthesis of L-lysine. 1. A method for the production of aspartate derived amino acids , preferably lysine , using a microorganism comprising at least the following properties , compared with the initial microorganism:(a) increased glucose 6-phosphate dehydrogenase activity,(b) increased activity of fructose 1,6-bisphosphatase,(c) attenuated isocitrate dehydrogenase activity,(d) increased diamionopimelate dehydrogenase activity, and(e) increased aspartate kinase activity.2. The method according to claim 1 , wherein said microorganism is a recombinant microorganism.3. The method according to claim 1 , wherein(a) the increased glucose-6-phosphate dehydrogenase activity is due to (i) overexpression of the zwf-gene, preferably based on the replacement of the natural promoter of the zwf-gene through a heterologous promoter and/or (ii) amino acid residue exchange A243T, or (iii) through the replacement of the natural promoter of the tkt-operon through a heterologous promoter,(b) the increased activity of fructose 1,6 is due to overexpression of the fbp-gene, preferably based on the replacement of the natural promoter through a heterologous promoter,(c) the attenuated isocitrate dehydrogenase activity is based on a replacement of the natural start codon of the icd-gene through a different start codon,(d) the increased diaminopimelate dehydrogenase activity is based on an overexpression of the ddh-gene, preferably through gene-multiplication,(e) the increased aspartate kinase ...

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Номер записи: 32
08-08-2013 дата публикации

PROCESS OF PRODUCING PHOSPHINOTHRICIN EMPLOYING NITRILASES

Номер: US20130204031A1
Автор: Albizati Kim F., Borer Bennett C., Grubbs Alan, Kambourakis Spiros
Принадлежит: STRATEGIC ENZYME APPLICATIONS, INC.

The present invention generally relates to processes for the enzymatic production of a phosphinothricin product or precursor thereof from a nitrile-containing substrate. 2. The process as set forth in wherein Rand Rare each hydrogen.3. The process as set forth in wherein Ris —C(O)Rand Ris hydrogen.4. The process as set forth in wherein Ris —C(O)Rand Ris substituted or unsubstituted C-Calkoxy.5. The process as set forth in wherein Ris Cor Calkoxy.6. The process as set forth in wherein Ris substituted or unsubstituted C-Calkyl claim 1 , substituted or unsubstituted aryl claim 1 , or an agronomically acceptable salt-forming cation.7. The process as set forth in wherein Ris a salt-forming ammonium cation.8. The process as set forth in wherein Ris C-Calkyl.9. The process as set forth in wherein Ris methyl or ethyl.10. The process as set forth in wherein Ris hydrogen.11. The process as set forth in wherein Rand Rare each hydrogen and Ris ethyl.12. The process as set forth in wherein Ris hydrogen claim 1 , Ris —C(O)R claim 1 , Ris ethyl claim 1 , and Ris hydrogen.13. The process as set forth in wherein Ris —C(O)Rand R claim 1 , R claim 1 , and Rare each hydrogen.14. The process as set forth in wherein Rand Rare part of a heterocyclic ring.15. (canceled)16. (canceled)18. (canceled)19. (canceled)20. The process as set forth in wherein the enzyme is selected from the group consisting of nitrilases claim 1 , nitrile hydratases claim 1 , a mixture of nitrile hydratases and amidases claim 1 , and mixtures thereof.21. The process as set forth in wherein the enzyme comprises a nitrilase.2225-. (canceled)26. The process as set forth in wherein the reaction mixture comprises an organism comprising the enzyme.27. (canceled)28. (canceled)29. The process as set forth in wherein the organism is a eukaryote.30A. thaliana, N. tabacum, B. campestris, B. napaus. The process as set forth in wherein the organism is selected from the group consisting of and mixtures thereof.31. The process as ...

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Номер записи: 33
29-08-2013 дата публикации

IMMOBILIZATION METHOD OF BIOACTIVE MOLECULES USING POLYPHENOL OXIDASE

Номер: US20130224795A1
Автор: Hyun Seung-Mi, Joung Yoon-ki, LEE Yun-Ki, Oh Ji-Hye, Park Ki-Dong, PARK Kyung-Min
Принадлежит: AJOU UNIVERSITY INDUSTRY-ACADEMIC COOPERATION FOUNDATION

A method is provided for immobilizing a bioactive molecule onto a surface using polyphenol oxidase. In the presence of polyphenol oxidase, a bioactive molecule containing a phenol or catechol group can be simply in situ oxidized within a short time to dopa or dopaquinone which forms a coordinate bond with a metal or polymer substrate, thus immobilizing the bioactive molecule onto the surface with stability. Based on the surface immobilization of bioactive molecules using polyphenol oxidase, various bioactive molecules such as osteogenetic peptides and growth factors can be simply immobilized to medical metal or polymer substrate surfaces such as orthopedic or dental implants which can be then effectively used to induce rapid osteogenesis after being transplanted. Also, antithrombotic agents and/or entothelialization inducing agents may be immobilized to medical substrates for vascular systems, such as stents and artificial blood vessels, thus guaranteeing hemocompatibility to the medical substrates. 1. A method for immobilization of a bioactive molecule on a surface , comprising:preparing a phenol-, catechol- or its derivative containing bioactive molecule (step 1); and treating a substrate surface with the bioactive molecule in presence of polyphenol oxidase to immobilize the bioactive molecule onto the surface (step 2).2. The method according to claim 1 , wherein the bioactive molecule contains a cell adhesion peptide containing a tyrosine.3. The method according to claim 2 , wherein the cell adhesion peptide is selected from the group consisting of peptides of SEQ ID NO. 1 (RGD-Y) claim 2 , SEQ ID NO. 2 (KQAGDV-Y) claim 2 , SEQ ID NO. 3 (YIGSR) claim 2 , SEQ ID NO. 4 (REDV-Y) claim 2 , SEQ ID NO. 5 (IKVAN-Y) claim 2 , SEQ ID NO. 6 (RNIAEIIKDI-Y) claim 2 , SEQ ID NO. 7 (KHIFSDDSSE-Y) claim 2 , SEQ ID NO. 8 (VPGIG-Y) claim 2 , SEQ ID NO. 9 (FHRRIKA-Y) claim 2 , SEQ ID NO. 10 (KRSR-Y) claim 2 , SEQ ID NO. 11 (NSPVNSKIPKACCVPTELSAI-Y) claim 2 , SEQ ID NO. 12 (APGL-Y) ...

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Номер записи: 34
29-08-2013 дата публикации

Method for Producing an L-Amino Acid Using a Bacterium of the Enterobacteriaceae Family

Номер: US20130224806A1
Автор: Nonaka Gen, Savrasova Ekaterina Alekseevna, Stoynova Natalia Viktorovna, Takumi Kazuhiro, Yamazaki Shunsuke
Принадлежит: AJINOMOTO CO., INC.

A method for producing an L-amino acid is described using a bacterium of the Enterobacteriaceae family, wherein the bacterium contains a protein which is able to confer resistance to growth inhibition by L-cysteine. 1. A method for producing an L-amino acid comprising:A) cultivating an Enterobacteriaceae bacterium that is able to produce an L-amino acid in a culture medium, andB) collecting the L-amino acid from the culture medium or the bacterium,wherein the bacterium has been modified to increase an activity of a protein which is able to confer to the bacterium resistance to growth inhibition by L-cysteine as compared to a non-modified bacterium, wherein said protein is selected from the group consisting of:(a) the protein of SEQ ID NO: 4 and(b) a protein having at least 95% sequence identity to the entire amino acid sequence of SEQ ID NO: 4.2. The method according to claim 1 , wherein expression of a DNA encoding said protein in said bacterium is enhanced as compared to a non-modified bacterium.3. The method according to claim 1 , wherein said bacterium is transformed with a DNA encoding said protein.4. The method according to claim 2 , wherein the DNA comprises a d0663 gene having the sequence of SEQ ID NO: 3.5. The method according to claim 1 , wherein said bacterium has been further modified to express a DNA encoding the protein of SEQ ID NO: 6 or a protein having at least 95% sequence identity to the entire amino acid sequence of SEQ ID NO: 6.6. The method according to claim 5 , wherein the DNA comprises a c09478 gene having the sequence of SEQ ID NO: 5.7. The method according to claim 1 , wherein said bacterium has been further modified to express a DNA encoding the protein of SEQ ID NO: 2 or a protein having at least 95% sequence identity to the entire amino acid sequence of SEQ ID NO: 2.8. The method according to claim 7 , wherein the DNA comprises a c0011 gene having the sequence of SEQ ID NO: 1.9. The method according to claim 5 , wherein said bacterium ...

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Номер записи: 35
05-09-2013 дата публикации

Microorganism producing L-methionine precursor and method of producing L-methionine and organic acid from the L-methionine precursor

Номер: US20130231503A1
Автор: Chang Jin-Sook, Cho Young-wook, Choi Kwang-myung, Choi Kyung-oh, KIM So-young, PARK YOUNG-HOON, Shin Yong-Uk, Um Hye-won
Принадлежит: CJ CHEILJEDANG CORPORATION

The present invention relates to a method for producing L-methionine, comprising: i) culturing an L-methionine precursor-producing microorganism strain in a fermentation solution, so that the L-methionine precursor accumulates in the solution; and ii) mixing a converting enzyme and methylmercaptan or its salts with at least a portion of the solution to convert the accumulated L-methionine precursor into L-methionine, as well as to microorganism strains used in each step. 1. A method for producing L-methionine , comprising:i) culturing an L-methionine precursor-producing microorganism strain in a fermentation solution, so that the L-methionine precursor accumulates in the solution; andii) mixing a converting enzyme and methylmercaptan or its salts with at least a portion of the solution to convert the accumulated L-methionine precursor into L-methionine.2. The method of claim 1 , wherein said the L-methionine precursor is an O-acylhomoserine.3EscherichiaErwiniaSerratiaProvidenciaCorynebacteriumPseudomonasLeptospiraSalmonellarBrevibacteriumHyphomonasChromobacteriumNocardia. The method of claim 1 , wherein the L-methionine precursor-producing microorganism strain of step i) is selected from the group consisting of sp. claim 1 , sp. claim 1 , sp. claim 1 , sp. claim 1 , sp. claim 1 , sp. claim 1 , sp. claim 1 , sp. claim 1 , sp. claim 1 , sp. claim 1 , sp. and sp. or fungi or yeasts.4EscherichiaCorynebacterium. The method of claim 3 , wherein the L-methionine precursor-producing microorganism strain is selected from sp. and sp.5Escherichia coli.. The method of claim 4 , wherein the L-methionine precursor-producing microorganism strain is6Corynebacterium glutamicum.. The method of claim 4 , wherein the L-methionine precursor-producing microorganism strain is7. The method of claim 1 , wherein the L-methionine precursor-producing microorganism strain is prepared by deleting or weakening the activity of cystathionine gamma synthase or O-succinylhomoserine sulfhydrylase or O ...

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Номер записи: 36
12-09-2013 дата публикации

RECOMBINANT BACTERIUM FOR L-HOMOSERINE PRODUCTION

Номер: US20130236934A1
Автор: Brinkhaus Friedhelm, Kang Ming, Lorbert Stephen, Ma Yingjie, Mahajan Aditya, McLaughlin Patrick, Peterson James C., Tata Muralidhar, Vakalapudi Sridhar, Wickard David
Принадлежит: NOVUS INTERNATIONAL INC.

The present invention encompasses a recombinant bacterium that is capable of producing L-homoserine and methods of using the bacterium for producing L-homoserine. 1E. coli. A recombinant bacterium for producing L-homoserine , the recombinant bacterium comprising:a. one or more exogenous nucleic acids encoding a polypeptide with aspartokinase activity,b. one or more exogenous nucleic acids encoding a polypeptide with homoserine dehydrogenase activity,c. one or more exogenous nucleic acids encoding a polypeptide with phosphoenolpyruvate carboxylase activity,d. one or more exogenous nucleic acids encoding a polypeptide with homoserine transport activity, ande. attenuated expression of the genomic nucleic acid encoding a polypeptide with homoserine kinase activity,wherein one or more of the exogenous nucleic acids are operably linked to a native promoter.2E. coli. A recombinant bacterium of claim 1 , wherein the one or more exogenous nucleic acids are introduced into the bacterium on a vector.3E. coli. A recombinant bacterium of claim 2 , wherein the vector is selected from the group consisting of a viral vector claim 2 , a cosmid claim 2 , a phage and a plasmid.4E. coli. A recombinant bacterium of claim 3 , wherein the vector is a plasmid.5E. coli. A recombinant bacterium of claim 4 , wherein the vector is an intermediate copy number plasmid.6E. coli. A recombinant bacterium of claim 5 , wherein the vector is pBR322.7E. coliE. coli. A recombinant bacterium of claim 1 , wherein the aspartokinase activity and homoserine dehydrogenase activity are encoded by the thrA nucleic acid.8E. coli. A recombinant acterium of claim 7 , wherein the aspartokinase activity and homoserine dehydrogenase activity are encoded by a mutant thrA nucleic acid encoding a polypeptide resistant to feedback inhibition.9E. coliE. coli. A recombinant bacterium of claim 1 , wherein the phosphoenolpyruvate carboxylase activity is encoded by the ppc nucleic acid.10E. coliE. coli. A recombinant ...

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Номер записи: 37
12-09-2013 дата публикации

PREPARATION OF 6-AMINOCAPROIC ACID FROM ALPHA-KETOPIMELIC ACID

Номер: US20130237698A1
Автор: Menke Hildegard Henna, Raemakers-Franken Petronella Catharina, Schürmann Martin, Trefzer Axel Christoph, Turk Stefanus Cornelis Hendrikus
Принадлежит: DSM IP ASSETS B.V.

The invention is directed to a method for preparing 6-aminocaproic acid, comprising decarboxylating alpha-aminopimelic acid, using at least one biocatalyst comprising an enzyme having alpha-aminopimelic acid decarboxylase activity. The invention is further directed to a method for preparing caprolactam from 6-aminocaproic acid prepared by said method, to a host cell suitable for use in a method according to the invention and to a polynucleotide encoding a decarboxylase that may be used in a method according to the invention. 1. Method for preparing 6-aminocaproic acid , comprising decarboxylating alpha-aminopimelic acid , using at least one biocatalyst comprising an enzyme having alpha-aminopimelic acid decarboxylase activity , wherein said enzyme comprises an amino acid sequence selected from the group of sequences represented by any of the SEQUENCE ID NO's: 2 , 5 , 8 and 11 and homologues of said sequences having alpha-aminopimelic acid decarboxylase activity.2. Method according to claim 1 , wherein said enzyme comprises a homologue having at least 40% claim 1 , preferably at least 60% claim 1 , in particular at least 80% claim 1 , more in particular at least 90% sequence identity with any of the SEQUENCE ID NO's: 2 claim 1 , 5 claim 1 , 8 and 11.3. Method according to claim 1 , comprising preparing alpha-aminopimelic acid from alpha-ketopimelic acid.4. Method according to claim 3 , wherein the preparation of alpha-aminopimelic acid is catalysed by a biocatalyst in the presence of an amino donor claim 3 , said biocatalyst having catalytic activity with respect to the transamination or the reductive amination of alpha-ketopimelic acid.5. Method according to claim 4 , wherein the biocatalyst comprises an enzyme having catalytic activity with respect to the transamination or the reductive amination of alpha-ketopimelic acid selected from the group of aminotransferases (E.C. 2.6.1) and amino acid dehydrogenases (E.C. 1.4.1).6. Method according to claim 5 , wherein the ...

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Номер записи: 38
03-10-2013 дата публикации

Compositions and Methods of Producing Methionine

Номер: US20130260424A1
Автор: Brazeau Brian, Chang Jin-Sook, Cho Kwang Myung, Cho Young Wook, Desouza Mervyn, JESSEN Holly J., KIM So-young, NIU Wei, Sanchez-Reira Fernando A., Shin Yong-Uk, Um Hyewon
Принадлежит: CJ CHEILJEDANG CORPORATION

Described herein are microorganisms that produce methionine and related products from endogenous genes in a transsulfuration pathway, as well as from exogenous genes providing a direct sulfhydrylation pathway. Novel genes that are useful for methionine and SAMe production are disclosed. 1. A microorganism comprising:one or more first peptides comprising direct sulfhydrylation activity (EC 2.5.1.49 and 4.2.99.-, wherein the direct sulfhydrylation activity uses as a substrate OSHS or OAHS; andone or more second peptides comprising transsulfuration activity (EC 2.5.1.48, and 4.4.1.8, wherein the direct sulfhydrylation activity consists of expression from an exogenous nucleic acid sequence.2E. coli.. The microorganism of claim 1 , wherein the microorganism is3. The microorganism of claim 1 , further comprising detectable amount of methionine.4. The microorganism of claim 1 , further comprising detectable amount of SAMe.5. The microorganism of claim 3 , wherein at least 10% of the methionine produced is from transsulfuration activity.6. The microorganism of claim 4 , wherein at least 10% of the SAMe produced is from transsulfuration activity.7. The microorganism of claim 3 , wherein at least 10% of the methionine produced is from direct sulfhydrylation activity.8. The microorganism of claim 4 , wherein at least 10% of the SAMe produced is from direct sulfhydrylation activity.9. The microorganism of claim 1 , further comprising a homoserine O-succinyltransferase peptide that is feed back resistance.10. The microorganism of claim 1 , further comprising a homoserine O-succinyltransferase peptide with GenBank Accession No: AAC76983 that has mutations in amino acid position 24 claim 1 , 29 claim 1 , 79 claim 1 , 114 claim 1 , 140 claim 1 , 163 claim 1 , 222 claim 1 , 275 claim 1 , 290 claim 1 , 291 claim 1 , 295 claim 1 , 297 claim 1 , 304 claim 1 , 305 claim 1 , or combinations thereof.11. The microorganism of claim 1 , further comprising a homoserine O-succinyltransferase ...

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Номер записи: 39
03-10-2013 дата публикации

Method for Producing an L-Amino Acid

Номер: US20130260425A1
Автор: Doi Hidetaka, Hoshino Yasushi, Masumitsu Yuri, Usuda Yoshihiro
Принадлежит:

A method for producing an L-amino acid includes culturing a bacterium which belongs to the family Enterobacteriaceae and has an L-amino acid-producing ability in a medium containing a carbon source selected from a fatty acid and an alcohol, and collecting the L-amino acid from the medium. A bacterium which has been subjected to a modification including at least one of enhancement of oxyS gene expression, enhancement of fixABC gene expression, and combination thereof, is used as the bacterium, or a substance that reduces intracellular hydrogen peroxide concentration of the bacterium is added to the medium. 1. A method for producing an L-amino acid , the method comprising:culturing a bacterium which belongs to the family Enterobacteriaceae and has an L-amino acid-producing ability, in a medium containing a carbon source selected from the group consisting of a fatty acid and an alcohol;reducing intracellular hydrogen peroxide concentration of the bacterium; andcollecting the L-amino acid from the medium.2. The method according to claim 1 , wherein reducing comprises modifying the bacterium so that the intracellular hydrogen peroxide concentration is reduced.3. The method according to claim 1 , wherein reducing comprises adding to said medium a substance that reduces intracellular hydrogen peroxide concentration of the bacterium.4Escherichia, PantoeaEnterobacter.. The method according to claim 1 , wherein the bacterium belongs to the genus claim 1 , or5Escherichia coli, Pantoea ananatisEnterobacter aerogenes.. The method according to claim 4 , wherein the bacterium is claim 4 , or6. The method according to claim 2 , wherein modifying the bacterium comprises a process selected from the group consisting of enhancement of oxyS gene expression claim 2 , enhancement of fixABC gene expression claim 2 , and combination thereof.7. The method according to claim 6 , wherein the oxyS gene encodes RNA having the nucleotide sequence of SEQ ID NO: 9 claim 6 , or a conservative ...

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Номер записи: 40
03-10-2013 дата публикации

BIOCATALYSTS AND METHODS FOR THE SYNTHESIS OF ARMODAFINIL

Номер: US20130260426A1
Автор: ALVIZO Oscar, Ang Ee Lui, Behrouzian Behnaz, Clay Michael, COLLIER Steven, Eberhard Ellen, Fu Fan Jaslyn, SMITH Derek, Song Shiwei, Widegren Magnus, Wilson Robert, Xu Junye, ZHU Jun
Принадлежит:

The present invention relates to non-naturally occurring polypeptides useful for preparing armodafinil, polynucleotides encoding the polypeptides, and methods of using the polypeptides. The non-naturally occurring polypeptides of the present invention are effective in carrying out biocatalytic conversion of the (i) 2-(benzhydrylsulfinyl)acetamide to (−)-2-[(R)-(diphenyl-methyl)sulfinyl]acetamide (armodafinil), or (ii) benzhydryl-thioacetic acid to (R)-2-(benzhydrylsulfinyl)acetic acid, which is a pivotal intermediate in the synthesis of armodafinil, in enantiomeric excess. 1. A non-naturally occurring polypeptide having cyclohexanone monooxygenase (CHMO) activity wherein the amino acid sequence of the polypeptide has at least 80% sequence identity to SEQ ID NO: 2 and one or more amino acid differences relative to SEQ ID NO: 2 selected from the following:X143C, E, F, G, H, K, M, P, Q, S, T, or W;X246A, E, G, I, L, N, P, S, T, or V;X277C, D, E, G, H, L, M, P, S, T, V, or W;X278A, C, G, H, K, N, Q, S, T, or V;X280L, T, or W;X281A, C, H, K, L, M, N, R, T, V, W, or Y;X326A, D, E, F, G, H, L, M, N, P, R, V, or W;X426G, Q, or T;X432E, I, K, N, Q, T, V, or W;X433 S;X435G, K, V, or Y;X490A, C, D, E, G, I, L, M, N, S, or Y; andX532M.2. The polypeptide of claim 1 , wherein the polypeptide is capable of converting the acid substrate compound (1b) to compound (2b) (R-enantiomer) or its opposite enantiomer compound (S-enantiomer) with at least 2-fold improved activity relative to the wild-type polypeptide of SEQ ID NO: 2.3. The polypeptide of claim 1 , wherein the amino acid sequence comprises one or more amino acid differences relative to SEQ ID NO: 2 selected from: X143G claim 1 , K claim 1 , M claim 1 , P claim 1 , Q claim 1 , S claim 1 , or W; X246A claim 1 , E claim 1 , G claim 1 , I claim 1 , L claim 1 , P claim 1 , S claim 1 , T claim 1 , or V; X278G claim 1 , or N; X426Q claim 1 , or T; X432E claim 1 , I claim 1 , L claim 1 , Q claim 1 , S claim 1 , T claim 1 , V claim 1 ...

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Номер записи: 41
03-10-2013 дата публикации

PROCESS FOR PRODUCING OPTICALLY ACTIVE ALPHA-METHYLCYSTEINE DERIVATIVE

Номер: US20130261331A1
Автор: HONDA Tatsuya, Inoue Kenji, Izumida Masashi, MORI Kohei, Nagashima Nabuo, Nanba Hirokazu, Ohishi Takahiro, Sugawara Masanobu, Yanagisawa Satohiro
Принадлежит:

The present invention provides a simple industrial process for producing an L- or D-optically active α-methylcysteine derivative or its salt, which is a useful pharmaceutical intermediate, from readily available, inexpensive raw materials. In a process for producing an L- or D-optically active α-methylcysteine derivative or its salt, a racemic N-carbamoyl-α-methylcysteine derivative or its salt is D-selectively cyclized with hydantoinase to produce a D-5-methyl-5-thiomethylhydantoin derivative or its salt and an N-carbamoyl-α-methyl-L-cysteine derivative or its salt, which are then subjected to deprotection of the amino group and the sulfur atom, and hydrolysis. 2Agrobacterium, BacillusPseudomonas.. The process according to claim 1 , wherein the hydantoinase is derived from microorganisms of the genus claim 1 , or3AgrobacteriumBacillusPseudomonas putida. The process according to claim 2 , wherein the hydantoinase is derived from sp. KNK712 (FERM BP-1900) claim 2 , sp. KNK245 (FERM BP-4863) claim 2 , or IFO12996.4. The process according to claim 1 , wherein the hydantoinase is used as an immobilized enzyme.5. The process according to claim 1 , wherein Ris a substituted or unsubstituted tertiary alkyl group having 4 to 15 carbon atoms.6. The process according to claim 5 , wherein the tertiary alkyl group is a tert-butyl group.8. The compound according to claim 7 , wherein Ris a tertiary alkyl group having 4 to 15 carbon atoms.9. The compound according to claim 8 , wherein the tertiary alkyl group is a tert-butyl group.11. The compound according to claim 10 , wherein Ris a tertiary alkyl group having 4 to 15 carbon atoms.12. The compound according to claim 11 , wherein the tertiary alkyl group is a tert-butyl group. This application is a divisional of 12/757,947 filed Apr. 9, 2010, which is a divisional of 10/515,658, filed Jan. 6, 2006 (now abandoned), which is a national stage of International Application No. PCT/JP03/07108 filed on Jun. 5, 2003 claiming priority to ...

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Номер записи: 42
10-10-2013 дата публикации

Method for Producing Carboxylic Acid Using Methanol-Assimilating Bacterium

Номер: US20130266993A1
Автор: Ishikawa Kohei, KONDO Kazuya, Murakoshi Yuriko
Принадлежит:

A method for producing a carboxylic acid by a fermentation process which comprises culturing a methanol-assimilating bacterium capable of producing the carboxylic acid in a liquid medium containing methanol and a counter ion to produce and accumulate the carboxylic acid in the medium, further comprising the feeding of a substance comprising methanol and a counter ion to the medium by fed-batch culturing to maintain the total ionic strength within the fermentation medium at or below a certain level. 1. A method for producing carboxylic acid by fermentation comprising ,A) culturing a methanol-assimilating bacterium that has an ability to produce the carboxylic acid in a liquid medium containing methanol and a counter ion,B) collecting the carboxylic acid from the medium or the bacterium,wherein a composition comprising methanol and a counter ion is fed to the medium by fed-batch culturing.2. The method of claim 1 , wherein said counter ion is a monovalent ion.3. The method according to claim 1 , wherein said counter ion is selected from the group consisting of ammonium chloride claim 1 , ammonium glutamate claim 1 , ammonium succinate claim 1 , ammonium fumarate claim 1 , ammonium aspartate claim 1 , and combinations thereof.4. The method according to claim 1 , wherein said carboxylic acid is an L-amino acid.5. The method according to claim 1 , wherein said L-amino acid is L-lysine.6Acromobacter, Pseudomonas, Protaminobacter, Methanomonas, Microcyclus, Methylobacillus, BacillusMethylophilus.. The method according to claim 1 , wherein said methanol-assimilating bacterium is of a genera selected from the group consisting claim 1 , and7. The method according to claim 1 , wherein said methanol-assimilating bacterium has been modified to increase the activity of an enzyme selected from the group consisting of diaminopimelate dehydrogenase claim 1 , diaminopimelate decarboxylase claim 1 , aspartate semialdehyde dehydrogenase claim 1 , and combinations thereof.8. The method ...

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Номер записи: 43
10-10-2013 дата публикации

TRANSAMINASE POLYPEPTIDES

Номер: US20130266994A1
Автор: Dhawan Ish K., Miller Gregory, Zhang Xiyun
Принадлежит:

The present disclosure provides engineered transaminase enzymes having improved properties as compared to a naturally occurring wild-type transaminase enzyme. Also provided are polynucleotides encoding the engineered transaminase enzymes, host cells capable of expressing the engineered transaminase enzymes, and methods of using the engineered transaminase enzymes to synthesize a variety of chiral compounds. 191-. (canceled)92. An engineered transaminase enzyme comprising a polypeptide comprising an amino acid sequence that is at least 90% identical to SEQ ID NO:2 and has an amino acid residue substitutions as compared to SEQ ID NO:2 at one or more residue positions selected from the group consisting of X57 , X85 , X86 , X153 , X228 , X233 , X297 , X317 , X318 , and X417 , wherein the polypeptide has transaminase activity.93. The engineered transaminase enzyme of claim 92 , wherein the one or more amino acid residue substitutions at positions X57 claim 92 , X85 claim 92 , X86 claim 92 , X153 claim 92 , X228 claim 92 , X233 claim 92 , X297 claim 92 , X317 claim 92 , X318 claim 92 , or X417 are selected from the group consisting of: X57 is claim 92 , A claim 92 , C claim 92 , F claim 92 , I claim 92 , L claim 92 , or S; X85 is A claim 92 , C claim 92 , S claim 92 , N claim 92 , T claim 92 , G claim 92 , or V; X86 is F claim 92 , S claim 92 , N claim 92 , A claim 92 , G claim 92 , or H; X153 is A claim 92 , C claim 92 , G claim 92 , N claim 92 , M claim 92 , Q claim 92 , S claim 92 , or T; X228 is G or T; X233 is L claim 92 , S claim 92 , I claim 92 , V claim 92 , N claim 92 , G claim 92 , or T; V297 is A claim 92 , S claim 92 , T claim 92 , I claim 92 , M claim 92 , Q claim 92 , C claim 92 , or G; X317 is L claim 92 , M claim 92 , or Y; X318 is G claim 92 , F claim 92 , C claim 92 , K claim 92 , W claim 92 , or R; and X417 is A claim 92 , C claim 92 , E claim 92 , F claim 92 , I claim 92 , N claim 92 , Q claim 92 , Y claim 92 , S claim 92 , T claim 92 , or V.94. The ...

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Номер записи: 44
24-10-2013 дата публикации

YEAST, YEAST EXTRACT CONTAINING GAMMA-GLU-ABU, AND A METHOD FOR PRODUCING THE SAME

Номер: US20130280381A1
Автор: HOSHINO Wataru, Ito Takayuki, MORITA Misato, NISHIUCHI Hiroaki, YAMAGISHI Kazuo, YAMAZAKI Junko
Принадлежит:

A yeast extract containing 0.2% or more of γ-Glu-Abu based on dry weight of the yeast extract is produced by culturing a yeast, such as or , in a medium containing a compound selected from Abu (L-2-aminobutyric acid) and γ-Glu-Abu (L-γ-glutamyl-L-2-aminobutyric acid), and preparing a yeast extract from the obtained cells. 1. A yeast extract containing 0.2% or more of γ-Glu-Abu based on dry weight of the yeast extract.2. A yeast extract according to claim 1 , which contains 0.5% or more of γ-Glu-Abu based on dry weight of the yeast extract.3. A yeast extract according to claim 1 , which contains 1.0% or more of γ-Glu-Abu based on dry weight of the yeast extract.4SaccharomycesCandida.. The yeast extract according to claim 1 , wherein the yeast belongs to the genus or5SaccharomycesCandida.. The yeast extract according to claim 2 , wherein the yeast belongs to the genus or6SaccharomycesCandida.. The yeast extract according to claim 3 , wherein the yeast belongs to the genus or7Saccharomyces cervisiaeCandida utilis.. The yeast extract according to claim 4 , which is obtained from or8Saccharomyces cervisiaeCandida utilis.. The yeast extract according to claim 5 , which is obtained from or9Saccharomyces cervisiaeCandida utilis.. The yeast extract according to claim 6 , which is obtained from or10. A method for producing a yeast extract containing γ-Glu-Abu claim 6 , which comprises culturing a yeast in a medium to which a compound selected from Abu and γ-Glu-Abu is added claim 6 , and preparing a yeast extract from the obtained cells.11. The method according to claim 10 , wherein the compound is added to the medium in an amount of 10 ppm or more in the case of Abu claim 10 , or 1 ppm or more in the case of γ-Glu-Abu claim 10 , and the yeast extract contains 0.2% or more of γ-Glu-Abu based on dry weight of the yeast extract.12SaccharomycesCandida.. The method according to claim 10 , wherein the yeast belongs to the genus or13SaccharomycesCandida.. The method according to ...

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Номер записи: 45
24-10-2013 дата публикации

HYBRID POLYKETIDE SYNTHASES

Номер: US20130280766A1
Автор: Fortman Jeffrey L., Hagen Andrew, Katz Leonard, Keasling Jay D., Poust Sean, Zhang Jingwei, Zotchev Sergey
Принадлежит: THE REGENTS OF THE UNVERSITY OF CALIFORNIA

The present invention provides for a polyketide synthase (PKS) capable of synthesizing an even-chain or odd-chain diacid or lactam or diamine. The present invention also provides for a host cell comprising the PKS and when cultured produces the even-chain diacid, odd-chain diacid, or KAPA. The present invention also provides for a host cell comprising the PKS capable of synthesizing a pimelic acid or KAPA, and when cultured produces biotin. 1. A non-naturally occurring polyketide synthase (PKS) capable of synthesizing an even-chain diacid.2. The PKS of claim 1 , wherein the even-chain diacid is not a compound synthesized by a naturally occurring PKS.3. The PKS of claim 1 , wherein the PKS is a hybrid PKS comprising modules claim 1 , domains claim 1 , and/or portions thereof from two or more PKSs.4Saccharopolyspora erythraea. The PKS of claim 3 , wherein the PKS comprises two modules claim 3 , wherein the first module comprises an aspartate-specific adenylation (A) domain claim 3 , modified to load succinate instead of aspartate claim 3 , from the non-ribosomal peptide synthetase (NRPS) pathway for calcium-dependent antibiotic (CDA) from linked to a peptidylcarrier protein (PCP) domain and a second module comprising a PKS ketosynthase (KS) domain claim 3 , wherein the PCP domain is capable of interacting with the KS domain.5Streptomyces verticillus.. The PKS of claim 4 , wherein the PCP and KS domains are the PCP and KS domains from the bleomycin pathway from6. The PKS of claim 4 , wherein the A domain is directly linked to the PCP domain.7. The PKS of claim 4 , wherein the second module comprises the KS domain fused to nystatin module 5 claim 4 , wherein the even-chain diacid produced is adipic acid.8. The PKS of claim 4 , wherein the A domain comprises the conserved aspartate residue (“Asp235”) changed to glutamine.9. The PKS of claim 3 , wherein the PKS comprises the loading domain of the chondrochloren PKS wherein the CoA ligase domain of the loading domain is ...

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Номер записи: 46
24-10-2013 дата публикации

COMPOSITION CONTAINING 2-ACYL-LYSOPHOSPHATIDYLSERINE AND METHOD FOR PRODUCING THE SAME

Номер: US20130281404A1
Автор: Gotoh Shoji, IMAMURA Shigeyuki, KAWASHIMA Junichi, Susa Tomoyuki, Tashiro Yasuhito, Yazawa Kazunaga
Принадлежит: Meiji Co., Ltd.

The present invention provides a method for producing a composition containing 2-acyl-lysophosphatidylserine, including (a) a step of obtaining a composition containing phosphatidylserine by allowing phospholipase D to act on a raw material containing phosphatidylcholine in the presence of serine and (b) a step of obtaining a composition containing 2-acyl-lysophosphatidylserine by allowing phospholipase A1 to act on the composition containing phosphatidylserine in the presence of one or more additives selected from the group consisting of the following (I), (II), and (III), in which (I) one or more salts selected from the group consisting of sulfate salts, phosphate salts, nitrate salts, citrate salts, and tartarate salts of monovalent cations, (II) a gum, and (III) an emulsifier. 115-. (canceled)16. A method for producing a composition containing 2-acyl-lysophosphatidylserine , comprising:(a) a step of obtaining a composition containing phosphatidylserine by allowing phospholipase D to act on a raw material containing phosphatidylcholine in the presence of serine; and(b) a step of obtaining a composition containing 2-acyl-lysophosphatidylserine by allowing phospholipase A1 to act on the composition containing phosphatidylserine in the presence of one or more additives selected from the group consisting of the following (I), (II), and (III):(I) one or more salts selected from the group consisting of sulfate salts, phosphate salts, nitrate salts, citrate salts, and tartarate salts of monovalent cations,(II) a gum, and(III) an emulsifier.17. A method for producing a composition containing 2-acyl-lysophosphatidylserine , comprising:(c) a step of obtaining a composition containing 2-acyl-lysophosphatidylcholine by allowing phospholipase A1 to act on a raw material containing phosphatidylcholine in the presence of one or more additives selected from the group consisting of the following (I), (II), and (III):(I) one or more salts selected from the group consisting of ...

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Номер записи: 47
31-10-2013 дата публикации

Methods of Pretreating Cellulosic Material with a Family 61 Polypeptide

Номер: US20130288296A1
Автор: Quinlan Jason, Xu Feng
Принадлежит: NOVOZYMES, INC.

The present invention relates to methods of degrading or converting a cellulosic material pretreated with a composition comprising one or more GH61 polypeptides. 1. A method of degrading a cellulosic material , comprising:(a) pretreating the cellulosic material with a composition comprising one or more GH61 polypeptides; and(b) saccharifying the GH61 polypeptide pretreated cellulosic material with an enzyme composition.2. The method of claim 1 , which further comprises treating the cellulosic material with a chemical pretreatment claim 1 , a physical pretreatment claim 1 , or a chemical pretreatment and a physical pretreatment.3. The method of claim 2 , wherein the pretreating with the one or more GH61 polypeptides is performed before claim 2 , during claim 2 , or after the chemical pretreatment claim 2 , the physical pretreatment claim 2 , or the chemical pretreatment and the physical pretreatment.4. The method of claim 1 , wherein the one or more GH61 polypeptides are inactivated following pretreatment of the cellulosic material.5. The method of claim 1 , wherein the enzyme composition comprises one or more enzymes selected from the group consisting of a cellulase claim 1 , a GH61 polypeptide having cellulolytic enhancing activity claim 1 , a hemicellulase claim 1 , an esterase claim 1 , an expansin claim 1 , a laccase claim 1 , a ligninolytic enzyme claim 1 , a pectinase claim 1 , a peroxidase claim 1 , a protease claim 1 , and a swollenin.6. The method of claim 1 , further comprising recovering the degraded cellulosic material.7. A method of producing a fermentation product claim 1 , comprising:(a) pretreating a cellulosic material with a composition comprising one or more GH61 polypeptides;(b) saccharifying the GH61 pretreated cellulosic material with an enzyme composition;(c) fermenting the saccharified cellulosic material with one or more fermenting microorganisms to produce the fermentation product; and(d) recovering the fermentation product from the ...

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Номер записи: 48
31-10-2013 дата публикации

Method of Producing L-Amino Acid

Номер: US20130288313A1
Автор: HAYASHI Kazuyuki, Matsui Kazuhiko, Nagai Yuri, Ueda Takuji, Usuda Yoshihiro
Принадлежит:

An L-amino acid is produced by culturing a microorganism belonging to the family Enterobacteriaceae having an L-amino acid-producing ability and modified so that glycerol dehydrogenase and dihydroxyacetone kinase activities are increased, in a medium containing glycerol as a carbon source to produce and accumulate an L-amino acid in the medium or cells, and collecting the L-amino acid from the medium or the cells. 1. A method for producing an L-amino acid , the method comprising:(A) providing a microorganism belonging to the family Enterobacteriaceae having an L-amino acid-producing ability and modified to increase glycerol dehydrogenase and dihydroxyacetone kinase activities,(B) culturing said microorganism in a medium containing glycerol as a carbon source to produce and accumulate an L-amino acid in the medium or cells, and(C) collecting the L-amino acid from the medium or the cells.2. The method according to claim 1 , wherein the glycerol dehydrogenase and dihydroxyacetone kinase activities are increased by increasing copy numbers of genes coding for glycerol dehydrogenase and dihydroxyacetone kinase claim 1 , or modifying expression control sequences of the genes.3. The method according to claim 1 , wherein the dihydroxyacetone kinase uses ATP as a phosphate donor.4. The method according to claim 1 , wherein the microorganism is further modified to increase glycerol uptake activity.5. The method according to claim 1 , wherein the microorganism is further modified to increase activity or activities of an enzyme selected from the group consisting of triosephosphate isomerase claim 1 , fructose bisphosphate aldolase claim 1 , fructose-1 claim 1 ,6-bisphosphatase claim 1 , fructose-6-phosphate aldolase claim 1 , and combinations thereof.6. The method according to claim 1 , wherein the microorganism is further modified to reduce activity or activities of glycerol kinase and/or membrane-binding type glycerol-3-phosphate dehydrogenase.7EscherichiaPantoea. The method ...

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Номер записи: 49
07-11-2013 дата публикации

Method for Producing a Target Substance by Fermentation

Номер: US20130295621A1
Автор: Nishio Yousuke, Yamada Kazuteru, Yamamoto Youko, Yokota Kosuke
Принадлежит:

A target substance can be produced by culturing a bacterium having an ability to produce 2-ketoglutaric acid or a derivative thereof, and an ability to produce xylonic acid from xylose, which is imparted with xylonate dehydratase activity, 2-keto-3-deoxyxylonate dehydratase activity and 2-ketoglutaric semialdehyde dehydrogenase activity, or in which these activities are enhanced, in a medium containing xylose as a carbon source to produce and accumulate the target substance in the medium, and collecting the target substance from the medium.

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Номер записи: 50
14-11-2013 дата публикации

Coryneform Bacterium Transformant and Process for Producing Aniline Using The Same

Номер: US20130302860A1
Автор: INUI MASAYUKI, Yukawa Hideaki
Принадлежит:

Provided is an aniline-producing transformant constructed by introducing a gene which encodes an enzyme having aminobenzoate decarboxylase activity into a coryneform bacterium as a host. Also provided is a process for producing aniline, which comprises a step of allowing the transformant to react in a reaction mixture containing aminobenzoic acid, an ester thereof, and/or a salt thereof under reducing conditions, and a step of recovering aniline from the reaction mixture. 1. An aniline-producing transformant constructed by introducing a gene which encodes an enzyme having aminobenzoate decarboxylase activity into a coryneform bacterium as a host.2Bacillus subtilisLactobacillus rhamnosusLactobacillus brevisPseudomonas putidaEscherichia coliSaccharomyces cerevisiaeEnterobacter cloacae.. The transformant of claim 1 , wherein the gene which encodes an enzyme having aminobenzoate decarboxylase activity is a gene derived from claim 1 , a gene derived from claim 1 , a gene derived from claim 1 , a gene derived from claim 1 , a gene derived from claim 1 , a gene derived from claim 1 , or a gene derived from3. The transformant of claim 1 , wherein the gene which encodes an enzyme having aminobenzoate decarboxylase activity is the DNA of the following (a) or (b):(a) a DNA consisting of the base sequence of SEQ ID NO: 16, SEQ ID NO: 19, SEQ ID NO: 22, SEQ ID NO: 25, SEQ ID NO: 28, SEQ ID NO: 31, or SEQ ID NO: 34(b) a DNA which hybridizes to a DNA consisting of a complementary base sequence of any of the DNAs of (a) under stringent conditions and which encodes a polypeptide having aminobenzoate decarboxylase activity.4Corynebacterium glutamicum.. The transformant of claim 1 , wherein the coryneform bacterium as the host is5Corynebacterium glutamicum. The transformant of claim 4 , wherein the coryneform bacterium as the host is R (FERM BP-18976) claim 4 , ATCC13032 claim 4 , or ATCC13869.6Corynebacterium glutamicumCorynebacterium glutamicum.. ANI-1 (Accession Number: NITE BP- ...

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Номер записи: 51
21-11-2013 дата публикации

Methods for Degrading or Converting Cellulosic Material

Номер: US20130309723A1
Автор: Huang Hongzhi, Ren Haiyu
Принадлежит: NOVZYMES A/S

Provided are methods for degrading or converting a cellulosic material, comprising: treating the cellulosic material with an enzyme composition in the presence of a polypeptide having catalase activity; and enzyme composition used for degrading or converting a cellulosic material comprising one or more (e.g., several) enzymes having cellulolytic and/or hemicellulolytic activity and a polypeptide having catalase activity. 125-. (canceled)26. A method for degrading or converting a cellulosic material , comprising: treating the cellulosic material with an enzyme composition in the presence of a polypeptide having catalase activity.27. The method of claim 26 , wherein the enzyme composition comprises one or more enzymes selected from the group consisting of a cellulase claim 26 , a GH61 polypeptide having cellulolytic enhancing activity claim 26 , a hemicellulase claim 26 , an esterase claim 26 , an expansin claim 26 , a laccase claim 26 , a ligninolytic enzyme claim 26 , a pectinase claim 26 , a peroxidase claim 26 , a protease claim 26 , and a swollenin.28. The method of claim 26 , wherein the cellulosic material is selected from the group consisting of agricultural residue claim 26 , herbaceous material claim 26 , municipal solid waste claim 26 , pulp and paper mill residue claim 26 , waste paper claim 26 , and wood; preferably claim 26 , arundo claim 26 , bagasse claim 26 , bamboo claim 26 , corn cob claim 26 , corn fiber claim 26 , corn stover claim 26 , miscanthus claim 26 , orange peel claim 26 , rice straw claim 26 , switchgrass claim 26 , wheat straw claim 26 , eucalyptus claim 26 , fir claim 26 , pine claim 26 , poplar claim 26 , spruce claim 26 , willow claim 26 , algal cellulose claim 26 , bacterial cellulose claim 26 , cotton linter claim 26 , filter paper claim 26 , microcrystalline cellulose claim 26 , or phosphoric-acid treated cellulose.29. The method of claim 26 , wherein the cellulosic material is pretreated claim 26 , especially by chemical ...

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Номер записи: 52
21-11-2013 дата публикации

Sensors For The Detection Of Intracellular Metabolites

Номер: US20130310458A1
Автор: BINDER Stephan, Bott Michael, EGGELING Lothar, Frunzke Julia, Mustafi Nurije
Принадлежит:

The present invention relates to a cell which is genetically modified with respect to its wild type and which comprises a gene sequence coding for an autofluorescent protein, wherein the expression of the autofluorescent protein depends on the intracellular concentration of a particular metabolite. 1. A cell which is genetically modified with respect to its wild type and which comprises a gene sequence coding for an autofluorescent protein , wherein the expression of the autofluorescent protein depends on the intracellular concentration of a particular metabolite.2. The cell according to claim 1 , wherein control of the expression of the gene sequence coding for the autofluorescent protein is effected as a function of the intracellular concentration of the particular metabolite at the transcription level.3. The cell according to or claim 1 , wherein the gene sequence coding for the autofluorescent protein is under the control of a heterologous promoter which claim 1 , in the wild type of the cell claim 1 , controls the expression of a gene of which the expression in the wild-type cell depends on the intracellular concentration of a particular metabolite.4. The cell according to claim 3 , wherein control of the expression of the gene sequence coding for the autofluorescent protein is effected as a function of the intracellular concentration of the particular metabolite at the translation level.5. The cell according to claim 2 , wherein the gene sequence coding for the autofluorescent protein is bonded functionally to a DNA sequence which claim 2 , at the mRNA level claim 2 , assumes the function of a riboswitch which regulates the expression of the gene sequence coding for the autofluorescent protein at the transcription level or the translation level.6CorynebacteriumEscherichia.. The cell according to or claim 2 , wherein the cell is a cell of the genus or7. The cell according to or claim 2 , wherein the metabolite is chosen from the group consisting of amino acids ...

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Номер записи: 53
28-11-2013 дата публикации

Process for the preparation of lacosamide

Номер: US20130317109A1
Автор: Cecilia Kvarnström Branneby, Margus Eek
Принадлежит: CAMBREX KARLSKOGA AB

There is provided a process for the preparation of Lacosamide (which is a useful medicament) of formula I, which comprises an enantioselective enzymatic acylation.

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Номер записи: 54
05-12-2013 дата публикации

PROCESS FOR PRODUCING TARGET SUBSTANCE BY FERMENTATION PROCESS

Номер: US20130323784A1
Автор: Abe Tetsuya, Ujihara Tetsuro, Yagasaki Makoto
Принадлежит: KYOWA HAKKO BIO CO., LTD.

A target substance can be efficiently produced by culturing, in a medium, a coryneform bacterium in which the activity of a PTS protein relating to fructose uptake is reduced or lost as compared with a parent strain and the bacterium can produce the target substance, allowing the target substance to form and accumulate in a culture; and collecting the target substance from the culture 1. A process for producing a target substance comprising:culturing in a medium a coryneform bacterium in which the activity of a PTS protein relating to fructose uptake is reduced or lost as compared with a parent strain, wherein the bacterium can produce the target substance;allowing the target substance to form and accumulate in a culture; andcollecting the target substance from the culture.2. The process according to claim 1 , wherein the reduced or lost activity of a PTS protein relating to fructose uptake is obtained by introducing a deletion claim 1 , a substitution claim 1 , or an addition of a base into a gene encoding the protein in the chromosomal DNA of the parent strain.3. The process according to claim 1 , wherein the PTS protein relating to fructose uptake is a protein containing FruK protein and FruA protein.46-. (canceled)7. The process according to claim 2 , wherein the PTS protein relating to fructose uptake is a protein containing FruK protein and FruA protein.8Corynebacterium glutamicum.. The process according to claim 1 , wherein the coryneform bacterium is9Corynebacterium glutamicum.. The process according to claim 2 , wherein the coryneform bacterium is10Corynebacterium glutamicum.. The process according to claim 3 , wherein the coryneform bacterium is11Corynebacterium glutamicum.. The process according to claim 7 , wherein the coryneform bacterium is12. The process according to claim 1 , wherein the target substance is an amino acid claim 1 , a peptide claim 1 , or a protein.13. The process according to claim 2 , wherein the target substance is an amino acid ...

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Номер записи: 55
05-12-2013 дата публикации

METHOD FOR PRODUCING CADAVERINE

Номер: US20130323800A1
Автор: Mimitsuka Takashi, Sasaki Nanami, Sawai Hideki, Sawai Kenji
Принадлежит: Toray Industries, Inc.

A method produces cadaverine more efficiently and at a higher yield than production methods by the conventional fermentation methods. The method includes culturing coryneform bacterium/bacteria having an ability to produce cadaverine and having a resistance to 2,2′-thiobis(ethylamine). Preferably, the coryneform bacterium/bacteria has/have lysine decarboxylase activity and, preferably, the coryneform bacterium/bacteria has/have homoserine auxotrophy and/or a resistance to S-(2-aminoethyl)-L-cysteine. 1. A method of producing cadaverine comprising culturing a coryneform bacterium/bacteria having an ability to produce cadaverine and having a resistance to 2 ,2′-thiobis(ethylamine).2. The method according to claim 1 , wherein said coryneform bacterium/bacteria has/have a resistance to 2 claim 1 ,2′-thiobis(ethylamine) having a concentration of not less than 250 mM.3. The method according to claim 1 , wherein said coryneform bacterium/bacteria has/have lysine decarboxylase activity.4CorynebacteriumBrevibacterium.. The method according to claim 1 , wherein said coryneform bacterium/bacteria is/are selected from the group consisting of genus and genus5. The method according to claim 1 , wherein said coryneform bacterium/bacteria has/have homoserine auxotrophy and/or a resistance to S-(2-aminoethyl)-L-cystein.6. The method according to claim 2 , wherein said coryneform bacterium/bacteria has/have lysine decarboxylase activity.7CorynebacteriumBrevibacterium.. The method according to claim 2 , wherein said coryneform bacterium/bacteria is/are selected from the group consisting of genus and genus8CorynebacteriumBrevibacterium.. The method according to claim 3 , wherein said coryneform bacterium/bacteria is/are selected from the group consisting of genus and genus9. The method according to claim 2 , wherein said coryneform bacterium/bacteria has/have homoserine auxotrophy and/or a resistance to S-(2-aminoethyl)-L-cystein.10. The method according to claim 3 , wherein said ...

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Номер записи: 56
12-12-2013 дата публикации

PROCESS FOR PRODUCTION OF CIS-4-HYDROXY-L-PROLINE

Номер: US20130330786A1
Автор: Hara Ryotaro, KINO Kuniki
Принадлежит: KYOWA HAKKO BIO CO., LTD.

Development of a method of economically and efficiently producing cis-4-hydroxy-L-proline. The present invention provides L-proline cis-4-hydroxylase. This enzyme may be derived from or . The present invention provides a method of producing cis-4-hydroxy-L-proline from L-proline by using this enzyme. The present invention provides a recombinant vector containing a polynucleotide encoding the enzyme and a transformant containing the vector. 1. A method of producing cis-4-hydroxy-L-proline , comprising the steps of:(A) providing a host organism that produces an enzyme protein selected from the group consisting of(1) the protein consisting of SEQ ID NO: 1 or 2,(2) a protein consisting of an amino acid sequence wherein one or several amino acids is/are deleted from, substituted in or added to the amino acid sequence of SEQ ID NO: 1 or 2, wherein the protein has L-proline cis-4-hydroxylase activity, and(3) a protein consisting of an amino acid sequence encoded by a polynucleotide that hybridizes under stringent conditions with the nucleic acid complement of SEQ ID NO: 3 or 4, wherein the protein has L-proline cis-4-hydroxylase activity and, wherein the stringent conditions comprise hybridization overnight in a solution of 6x saline-sodium citrate (SSC) and 0.2% sodium dodecyl sulfate (SDS) at 65 ° C., washing two times with a solution of 1×SSC and 0.1% SDS at 65 ° C. for 30 minutes, and washing two times with a solution of 0.2×SSC and 0.1% SDS at 65 ° C. for 30 minutes,(B) contacting the host organism with L-proline in a reaction system to produce cis-4-hydroxy-L-proline, and(C) recovering cis-4-hydroxy-L-proline from the reaction system.2. The method of claim 1 , wherein the protein consists of SEQ ID NO: 1 or 2.3. The method of claim 1 , wherein the protein consists of an amino acid sequence wherein one or several amino acids is/are deleted from claim 1 , substituted in claim 1 , or added to the amino acid sequence of SEQ ID NO: 1 or 2 claim 1 , wherein the protein has ...

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Номер записи: 57
12-12-2013 дата публикации

METHOD FOR PRODUCING CHEMICAL BY CONTINUOUS FERMENTATION

Номер: US20130330787A1
Автор: Cheon Jihoon, Kanamori Satoko, Mimitsuka Takashi, Nishida Makoto, Takeuchi Norihiro, Tanaka Yuji
Принадлежит:

A method produces a chemical through continuous fermentation including: (a) culturing a cell in a culture medium in a fermentor to ferment a feedstock to produce a chemical; (b) conducting filtration of the culture medium with a separation membrane module; (c) separating a permeate containing the chemical from the culture medium while retaining a non-permeated liquid in the fermentor, and (d) supplying a gas from at least one of a lower portion of the separation membrane module and a pipe communicating between the fermentor and the separation membrane module to adjust a gas linear velocity in the separation membrane module to 0.15 cm/s to 70 cm/s while supplying the separation membrane module with a liquid. 1. A method of producing a chemical through continuous fermentation comprising:(a) culturing a cell in a culture medium in a fermentor to ferment a feedstock to produce a chemical;(b) conducting filtration of the culture medium with a separation membrane module;(c) separating a permeate containing the chemical from the culture medium while retaining a non-permeated liquid in the fermentor, and(d) supplying a gas from at least one of a lower portion of the separation membrane module and a pipe communicating between the fermentor and the separation membrane module to adjust a gas linear velocity in the separation membrane module to 0.15 cm/s to 70 cm/s while supplying the separation membrane module with a liquid.2. The method according to claim 1 , wherein in (d) claim 1 , the gas contains oxygen.3. The method according to claim 2 , further comprising claim 2 , in addition to (d) claim 2 , (e) supplying the fermentor with a gas claim 2 , wherein:the gas is supplied in (d) intermittently, andwhen the gas is not supplied in (d), a supply rate of the gas in (e) is increased compared with that when the gas is supplied in (d).4. The method according to claim 1 , wherein the filtration in (b) is conducted intermittently.5. The method according to claim 1 , wherein the ...

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Номер записи: 58
19-12-2013 дата публикации

Amidase and Use Thereof for Producing 3-Aminocarboxylic Acid Esters

Номер: US20130337512A1
Автор: Friedrich Thomas, HAUER BERNHARD, Krahnert Wolf-Rüdiger, Krauser Susanne, Schneider Nina, Stürmer Rainer
Принадлежит:

Process for producing optically active 3-aminocarboxylic acid ester compounds of general Formula I, and the ammonium salts thereof, 4. The process according to claim 1 , wherein a β-ketoester of Formula I.1 is reacted with at least one carboxylic acid amide of formula R—C(O)NH claim 1 , in the presence of an amidation catalyst claim 1 , with removal of the reaction water claim 1 , to a 3-aminocarboxylic acid ester of Formula I.a.5. The process according to claim 2 , wherein a β-ketoester of Formula I.1 is reacted with at least one carboxylic acid amide of formula R—C(O)NH claim 2 , in the presence of an amidation catalyst claim 2 , with removal of the reaction water claim 2 , to a 3-aminocarboxylic acid ester of Formula I.a.6. The process according to claim 1 , wherein the deacylation is carried out in aqueous buffer as reaction medium.7. The process according to claim 2 , wherein the deacylation is carried out in aqueous buffer as reaction medium.8. The process according to claim 3 , wherein the hydrogenation b) is carried out in the presence of a hydrogenation catalyst claim 3 , which comprises at least one complex of a transition metal of groups 8 to 11 of the periodic table of the elements and comprises claim 3 , as ligand claim 3 , at least one chiral claim 3 , phosphorus atom-containing compound.9. The process according to claim 3 , wherein Rstands for phenyl and Rand Rhave the meanings stated in . This application is a divisional of U.S. application Ser. No. 13/497,985, filed Mar. 23, 2012, which is a national stage application (under 35 U.S.C. §371) of PCT/EP2010/064098, filed Sep. 24, 2010, which claims benefit of European Application No. 09171414.7, filed Sep. 25, 2009, the entire contents of each of which are hereby incorporated by reference in this application.The Sequence Listing associated with this application is filed in electronic format via EFS-Web and is hereby incorporated by reference into the specification in its entirety. The name of the text ...

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Номер записи: 59
26-12-2013 дата публикации

MICROBES WITH AN IMPROVED ABILITY TO PRODUCE ORNITHINE AND METHOD FOR PRODUCING ORNITHINE USING SAME

Номер: US20130344545A1
Автор: Choi Hyang, Choi Su Jin, Jhon Sung Hoo, Kang Min Sun, Lee Han Won, Lee Kyoung Min, Shin Soo An, Um Hye Won
Принадлежит: CJ CHELJEDANG CORPORATION

The present invention relates to a microorganism having an improved ornithine-producing ability, in which the biosynthetic pathway of arginine form ornithine is blocked, the intracellular glutamate level is increased, and the biosynthetic pathway of ornithine from glutamate is enhanced, and a method for producing ornithine using the microorganism. 1. A microorganism having an improved ornithine-producing ability , wherein the activities of ornithine carbamoyltransferase and a protein involved in glutamate export (NCgl1221) are modified to be attenuated , compared to their endogenous activities.2. The microorganism according to claim 1 , wherein the ornithine carboyltransferase has an amino acid sequence of SEQ ID NO. 18 claim 1 , or an amino acid sequence having 70% or more homology with the sequence.3. The microorganism according to claim 1 , wherein the protein involved in glutamate export has an amino acid sequence of SEQ ID NO. 20 claim 1 , or an amino acid sequence having 70% or more homology with the sequence.4. The microorganism according to claim 1 , wherein the activity of the ornithine carboyltransferase and the protein involved in glutamate export is attenuated by a method selected from the group consisting of (1) a partial or full deletion of a gene coding for the protein claim 1 , (2) modification of an expression regulatory sequence for suppressing the gene expression claim 1 , (3) modification of the gene sequence on chromosome for diminishing the protein activity claim 1 , and 4) a combination thereof.5. The microorganism according to claim 1 , wherein activities of acetyl gamma glutamyl phosphate reductase (ArgC) claim 1 , acetylglutamate synthase or ornithine acetyltransferase (ArgJ) claim 1 , acetylglutamate kinase (ArgB) and acetylornithine aminotransferase (ArgD) are further enhanced claim 1 , compared to their endogenous activities.6. The microorganism according to claim 5 , wherein each of ArgC claim 5 , ArgJ claim 5 , ArgB claim 5 , and ArgD ...

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Номер записи: 60
02-01-2014 дата публикации

METHOD FOR PRODUCING CADAVERINE

Номер: US20140004576A1
Автор: Mimitsuka Takashi, Sasaki Nanami, Sawai Hideki, Sawai Kenji
Принадлежит: Toray Industries, Inc.

A method of producing cadaverine is more efficient and at a higher yield than production methods by the conventional fermentation methods. The method includes culturing coryneform bacterium/bacteria having a resistance to a pH of 5.5 or less. Preferably, the coryneform bacterium/bacteria has/have lysine decarboxylase activity and, preferably, the coryneform bacterium/bacteria has/have homoserine auxotrophy and/or a resistance to S-(2-aminoethyl)-L-cysteine. 1. A method of producing cadaverine , said method comprising culturing a coryneform bacterium/bacteria having a resistance to a pH of 5.5 or less.2. The method according to claim 1 , wherein said coryneform bacterium/bacteria has/have lysine decarboxylase activity.3CorynebacteriumBrevibacterium.. The method according to claim 1 , wherein said coryneform bacterium/bacteria is/are selected from the group consisting of genus and genus4. The method according to claim 1 , wherein said coryneform bacterium/bacteria has/have homoserine auxotrophy and/or a resistance to S-(2-aminoethyl)-L-cystein.5CorynebacteriumBrevibacterium.. The method according to claim 2 , wherein said coryneform bacterium/bacteria is/are selected from the group consisting of genus and genus6. The method according to claim 2 , wherein said coryneform bacterium/bacteria has/have homoserine auxotrophy and/or a resistance to S-(2-aminoethyl)-L-cystein.7. The method according to claim 3 , wherein said coryneform bacterium/bacteria has/have homoserine auxotrophy and/or a resistance to S-(2-aminoethyl)-L-cystein. This disclosure relates to a method of producing cadaverine by using coryneform bacterium/bacteria having an ability to produce cadaverine.Cadaverine has a diamine structure, and is also called 1,5-pentanediamine or pentamethylenediamine and so on. Since cadaverine has recently been focused on as a raw material monomer for polyamide, mass production of cadaverine is demanded. Known examples of the method of producing cadaverine include a ...

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Номер записи: 61
02-01-2014 дата публикации

MICROORGANISMS FOR PRODUCING PUTRESCINE AND METHOD FOR PRODUCING PUTRESCINE USING SAME

Номер: US20140004577A1
Автор: Choi Hyang, Choi Su Jin, Jhon Sung Hoo, Kang Min Sun, Lee Han Won, Lee Kyoung Min, Shin Soo An, Um Hye Won
Принадлежит: CJ CHEILJEDANG CORPORATION

The present invention relates to a putrescine-producing microorganism and a method for producing putrescine using the same. To be more specific, the present invention is directed to a microorganism given the ability to produce putrescine which is generated by blocking a biosynthetic pathway from ornithine to arginine, increasing the intracellular level of glutamate, enhancing the biosynthetic pathway of ornithine from glutamate, and introducing extracellular ornithine decarboxylase; and a method for producing putrescine by using the microorganism. 1. A putrescine-producing microorganism , wherein the microorganism is modified to have weakened activities of an ornithine carbamoyltransferase and a protein involved in glutamate export (NCgl1221) compared to the endogenous activities thereof , and an activity of ornithine decarboxylase (ODC) is introduced into the microorganism.2. The putrescine-producing microorganism of claim 1 , wherein the ornithine carbamoyltransferase has an amino acid sequence of SEQ ID No. 28 or an amino acid sequence having 70% or more homology thereto.3. The putrescine-producing microorganism of claim 1 , wherein the protein involved in glutamate export has an amino acid sequence of SEQ ID No. 30 or an amino acid sequence having 70% or more homology thereto.4. The putrescine-producing microorganism of claim 1 , wherein the activity of the ornithine carbamoyltransferase and the protein involved in glutamate export is weakened by a method selected from the group consisting of (1) a partial or full deletion of a gene coding for the protein claim 1 , (2) modification of an expression regulatory sequence for suppressing the gene expression claim 1 , (3) modification of the gene sequence on chromosome for weakening the protein activity claim 1 , and 4) a combination thereof.5. The putrescine-producing microorganism of claim 1 , wherein the ornithine decarboxylase has an amino acid sequence of SEQ ID No. 41 or an amino acid sequence having 70% or ...

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Номер записи: 62
16-01-2014 дата публикации

SYSTEM FOR PRODUCING L-HOMOPHENYLALANINE AND A PROCESS FOR PRODUCING L-HOMOPHENYLALANINE

Номер: US20140017738A1
Автор: ABD. SHUKOR Syamsul Rizal, AHMAD Abdul Latif, OH Pei Ching
Принадлежит: Universiti Sains Malaysia

The present invention relates to a system for producing L-homophenylalanine and a process for producing L-homophenylalanine using the system. The system and the process include monitoring and controlling of the reaction conditions (e.g., temperature and pH) to desired or predetermined values. The monitoring, adjusting and agitating steps provided by the method thereby result in a more complete conversion of the available substrate and produce a sufficient yield of L-homophenylalanine. 1. A process for producing L-homophenylalanine comprising the steps of:(a) dissolving 2-oxo-4-phenylbutanoic acid, 1,4-dithiothreitol, sodium formate and NADH in deionized water at a pH of between 6 to 10 with an addition of a hydroxide;(b) adding L-phenylalanine dehydrogenase and formate dehydrogenase into a solution obtained from step (a);(c) stirring a solution obtained from step (b) at a temperature of between 27° C. to 50° C. in an inert atmosphere;(d) separating and collecting of biocatalysts from a solution obtained from step (c);(e) acidifying a solution obtained from step (d);(f) filtering white precipitate obtained from step (e);(g) washing the white precipitate from step (f) with a non-reacting liquid; and(h) drying the white precipitate from step (g).2. The process as claimed in claim 1 , wherein the hydroxide used in step (a) is ammonium hydroxide.3. The process as claimed in claim 2 , wherein ammonium hydroxide used is 1 N ammonium hydroxide.4. The process as claimed in claim 1 , wherein the solution in step (e) is acidified to pH 5.5 in the second vessel.5. The process as claimed in claim 1 , wherein the non-reacting liquid is water claim 1 , preferably distilled water.6. The process as claimed in claim 1 , wherein step (h) is conducted in vacuum.7. The process as claimed in claim 1 , wherein said L-homophenylalanine has an enantiomeric excess of over 99%. This application is a Divisional of co-pending U.S. patent application Ser. No. 13/388,915, filed on Feb. 3, 2012, ...

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Номер записи: 63
23-01-2014 дата публикации

MICROORGANISM HAVING ENHANCED L-AMINO ACIDS PRODUCTIVITY AND PROCESS FOR PRODUCING L-AMINO ACIDS USING THE SAME

Номер: US20140024087A1
Автор: Hwang Young Bin, LEE Keun Chul, Lee Kwang Ho, Lee Seok Myung
Принадлежит: CJ CHEILJEDANG CORPORATION

A microorganism of the genus having enhanced L-amino acid productivity, wherein the microorganism is transformed to have an enhanced NAD kinase activity and an inactivated activity of an enzyme having an amino acid sequence of SEQ ID NO: 2 encoded by tehB gene and a method for producing L-amino acids using the microorganism of the genus 1Escherichia. A microorganism of the genus having enhanced L-amino acid productivity , wherein the microorganism is transformed to have an enhanced NAD kinase activity and an inactivated activity of an enzyme having an amino acid sequence of SEQ ID NO: 2 encoded by tehB gene.2. The microorganism according to claim 1 , wherein the NAD kinase is a protein having an amino acid sequence of SEQ ID NO: 4.3. The microorganism according to claim 1 , wherein the NAD kinase activity is enhanced by one or more methods of increasing the copy number by chromosomal insertion or vector introduction claim 1 , substitution or modification of the expression-regulatory region claim 1 , and gene mutation.4. The microorganism according to claim 1 , wherein the inactivation is performed by one or more methods of deletion of a part or the entire of the gene by homologous recombination claim 1 , suppression of enzyme expression by transposon insertion within the corresponding gene claim 1 , and suppression of enzyme expression by insertion of antibiotic resistance genes.5EscherichiaE. coli.. The microorganism according to claim 1 , wherein the microorganism of the genus is6. The microorganism according to claim 1 , wherein the L-amino acid is L-threonine or L-tryptophan.7Escherichia. The microorganism according to claim 6 , wherein the microorganism of the genus is provided with sucrose assimilation ability.8EscherichiaE. coli. The microorganism according to claim 1 , wherein the microorganism of the genus is an L-threonine-producing claim 1 , CA03-448 having Deposit No. KCCM11167P or CA03-449 having Deposit No. KCCM11168P.9EscherichiaE. coli. The ...

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Номер записи: 64
13-02-2014 дата публикации

Method for Producing Substance Utilizing Microorganism

Номер: US20140045219A1
Автор: Hisao Ito, Kazuo Nakanishi, Osamu Kurahashi, Yoshio Kawahara, Yuta Nakai
Принадлежит: Ajinomoto Co Inc

In a method for producing a target substance utilizing a microorganism comprising culturing the microorganism in a medium to produce and accumulate the target substance in the medium and collecting the target substance, microorganism is employed, which is a mutant strain or a genetic recombinant strain constructed from a parent strain of the microorganism having a respiratory chain pathway of high energy efficiency and a respiratory chain pathway of low energy efficiency as respiratory chain pathways, and having either one or both of the following characteristics: (A) the respiratory chain pathway of high energy efficiency is enhanced, (B) the respiratory chain pathway of low energy efficiency is deficient.

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Номер записи: 65
13-02-2014 дата публикации

Method for Producing L-Amino Acid

Номер: US20140045228A1
Автор: Kazuhiko Matsui, Yoshihiro Usuda
Принадлежит: Ajinomoto Co Inc

An L-amino acid is produced by culturing an Enterobacteriaceae which is able to produce an L-amino acid in a medium containing glycerol, especially crude glycerol, as the carbon source to produce and accumulate the L-amino acid in the culture, and collecting the L-amino acid from the culture.

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Номер записи: 66
20-02-2014 дата публикации

BETAINE ESTERS AND PROCESS FOR MAKING AND USING

Номер: US20140050687A1
Автор: Boaz Neil Warren, Burk Christopher Harlan, Clendennen Stephanie Kay
Принадлежит: Estman Chemical Company

A variety of betaine esters, including dialkylaminoalkyl cocoate betaines and dialkylaminoalkyl hydrogenated cocoate betaines are disclosed. These betaines can be advantageously prepared in high yield and purity by a three-step transiterification chemoenzymatic process or a two-step direct esterficiation chemoenzymatic process. These betaine esters have excellent surfactant properties. 2. The compound according to claim 1 , wherein A is selected from the group consisting of C-Calkylene and C-Calkenylene.3. The compound according to claim 1 , wherein Ris methyl.4. The compound according to claim 1 , wherein R is selected from the group consisting of C-Calkyl and mixtures thereof claim 1 , Ris methyl claim 1 , and A is 1 claim 1 ,3-propylene.5. The compound according to wherein the compound is selected from the group consisting of 3-dimethylaminopropyl hydrogenated cocoate (R is a mixture of C-C) betaine claim 1 , 3-dimethylaminopropyl hydrogenated stripped cocoate (R is a mixture of C-C) betaine claim 1 , 3-dimethylaminopropyl laurate betaine claim 1 , 3-dimethylaminopropyl myristate betaine claim 1 , and 3-dimethylaminopropyl palmitate betaine.6. A surfactant comprising the compound according to .7. A formulated product comprising a compound according to .8. The product according to claim 6 , wherein said compound is present in an amount of from about 0.001 weight % to about 20 weight %.9. The product according to claim 7 , wherein the compound is present in an amount of from about 0.01 weight % to about 15 weight %.11. The method according to claim 10 , wherein R is selected from the group consisting of C-Calkyl and mixtures thereof claim 10 , Ris methyl claim 10 , Ris selected from the group consisting of C-Calkyl claim 10 , and A is selected from the group consisting of C-Calkylene and C-Calkenylene.12. The method according to claim 10 , wherein the ester is produced by solvolysis of non-hydrogenated or hydrogenated triglycerides in the presence of a lower ...

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Номер записи: 67
20-02-2014 дата публикации

Method for Producing an L-Amino Acid Belonging to the Glutamate Family, Using a Coryneform Bacterium

Номер: US20140051132A1
Автор: Gusyatiner Mikhail Markovich, Rostova Yulia Georgievna, Samsonov Viktor Vasilievich, Samsonova Svetlana Alekseevna
Принадлежит: AJINOMOTO CO., INC.

The present invention provides a method for producing an L-amino acid belonging to the glutamate family, using a coryneform bacterium which has been modified so that expression of one or more gene(s) of the NCgl_2067-NCgl_2065 operon in said bacterium is/are attenuated. 1. A coryneform bacterium which is able to produce an L-amino acid belonging to the glutamate family , wherein said bacterium has been modified to attenuate the expression of one or more gene(s) of the NCgl2067-NCgl2065 operon.2. The bacterium according to claim 1 , wherein said bacterium has been modified to attenuate the expression of the NCgl2067 gene.3. The bacterium according to claim 2 , wherein said expression of the NCgl2067 gene is attenuated by inactivation of the NCgl2067 gene.4. The bacterium according to claim 1 , wherein said bacterium has been modified to attenuate the expression of the NCgl2066 gene.5. The bacterium according to claim 4 , wherein said expression of the NCgl2066 gene is attenuated by inactivation of the NCgl2066 gene.6CorynebacteriumBrevibacterium.. The bacterium according to claim 1 , wherein said bacterium belongs to the genus or7Brevibacterium flavum.. The bacterium according to claim 6 , wherein said bacterium is8. The bacterium according to claim 1 , wherein said L-amino acid is selected from the group consisting of L-glutamic acid claim 1 , L-glutamine claim 1 , L-proline claim 1 , L-histidine claim 1 , L-arginine claim 1 , L-ornithine claim 1 , L-citrulline claim 1 , and combinations thereof.9. The bacterium according to claim 8 , wherein said L-amino acid is selected from the group consisting of L-glutamic acid claim 8 , L-glutamine claim 8 , and combinations thereof.10. A method for producing an L-amino acid belonging to the glutamate family comprising:{'claim-ref': {'@idref': 'CLM-00001', 'claim 1'}, 'cultivating the bacterium according to in a medium, and'}collecting said L-amino acid from the medium.11. The method according to claim 10 , wherein said L- ...

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Номер записи: 68
20-02-2014 дата публикации

Ketol-acid reductoisomerase enzymes and methods of use

Номер: US20140051133A1
Автор: Alexander Vincent Tobias, Daniel P. O'keefe, Der-Ing Liao, Jeremy Stephen Minshull, Sridhar Govindarajan, Steven Cary Rothman, Yougen Li
Принадлежит: BUTAMAX ADVANCED BIOFUELS LLC

Provided herein are polypeptides having ketol-aid reductoisomerase activity as well as microbial host cells comprising such polypeptides. Polypeptides provided herein may be used in biosynthetic pathways, including, but not limited to, isobutanol biosynthetic pathways.

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Номер записи: 69
06-03-2014 дата публикации

PRODUCTION OF ENANTIOMERICALLY PURIFIED AMINO ACIDS

Номер: US20140065679A1
Автор: Baxter Scott, Campopiano Dominic, Holt-Tiffin Karen Elizabeth
Принадлежит:

The present application relates to a mutated sp. TS-1-60 NAAAR that shows improved activity of the enzyme compared with the wild type sp. TS-1-60 NAAAR. The mutated NAAAR is almost five times more active than its wild type counterpart. The present application also relates to the use of mutated sp. TS-1-60 NAAAR in the production of enantiomerically pure amino acid from its N-acyl derivative via dynamic kinetic resolution method. 1. N-acyl amino acid racemase (NAAAR) comprising an amino acid sequence that is at least 90% identical to SEQ ID No. 1.2Amycolatopsis. The NAAAR of claim 1 , wherein NAAAR is mutated sp. TS-1-60 NAAAR of SEQ. ID No. 1.3. A process for the preparation of enantiomerically pure amino acids comprising treating acyl derivative of an amino acid with NAAAR having an amino acid sequence that is at least 90% identical to SEQ ID No. 1 and an acylase enzyme.4. The process of claim 3 , wherein the reaction is performed at about 20° C. to about 80° C.5. The process of claim 4 , wherein the reaction is performed at about 30° C. to about 70° C.6. The process of claim 3 , wherein the reaction is performed at a pH of about 7.5 to about 9.7. The process of claim 6 , wherein the reaction is performed at a pH of about 8.8. The process of claim 3 , wherein acyl derivative of amino acid comprises one to four carbon atoms in the acyl group.9. The process of claim 8 , wherein the acyl group is an acetyl group.10. The process of claim 3 , wherein the substrate concentration is about 300 mM.11. The process of claim 3 , wherein the substrate concentration is at least about 50 mM.12. The process of claim 3 , wherein amino acid is selected from a group of D-methionine claim 3 , L-methionine claim 3 , D-alanine claim 3 , L-alanine claim 3 , D-leucine claim 3 , L-leucine claim 3 , D-phenyalanine claim 3 , L-phenylalanine claim 3 , D-isoleucine claim 3 , L-isoleucine claim 3 , D-valine claim 3 , L-valine claim 3 , D-tryptophan claim 3 , L-tryptophan claim 3 , D-aspartic ...

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Номер записи: 70
20-03-2014 дата публикации

Method for Producing a Target Substance by Fermentation

Номер: US20140080185A1
Автор: Abe Kenji, Kadotani Naoki, Takeshita Ryo
Принадлежит: AJINOMOTO CO., INC.

A method is described for producing a target substance utilizing a microorganism by culturing the microorganism in a medium to produce and accumulate the target substance in the medium, and then collecting the target substance from culture. The microorganism is imparted with isomaltase activity, or modified to increase isomaltase activity. 1. A method for producing an L-amino acid or a nucleic acid utilizing a microorganism , which comprises:A) culturing the microorganism in a medium, andB) collecting the L-amino acid or the nucleic acid from the medium,wherein the microorganism has been modified so that: A) it comprises isomaltase activity, and/or B) the isomaltase activity is increased, and wherein said activity causes the decomposition of phosphorylated isomaltose into glucose and glucose phosphate.2. The method according to claim 1 , wherein the microorganism has been further modified so that:A) it is able to take up isomaltose, and/orB) the activity to take up isomaltose is increased.3. The method according to claim 1 , wherein the microorganism has been further modified so that:A) it comprises maltase activity, and/orB) the maltase activity is increased.4. The method according to claim 3 , wherein the microorganism has been further modified so that:A) it is able to take up maltose, and/orB) the activity to take up maltose is increased.5. The method according to claim 1 , wherein the medium contains a component selected from the group consisting of:A) isomaltose, andB) isomaltose and maltose.6Bacillus. The method according to claim 1 , wherein the microorganism comprises a gene coding for isomaltase of a bacterium.7. The method according to claim 6 , wherein the isomaltase is selected from the group consisting of:(A) a protein comprising the amino acid sequence shown in SEQ ID NO: 40,(B) a protein comprising the amino acid sequence shown in SEQ ID NO: 40, but wherein one or several amino acid residues are substituted, deleted, inserted or added, and the protein ...

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Номер записи: 71
20-03-2014 дата публикации

METHOD FOR PRODUCING L-CYSTINE BY FERMENTATION UNDER CONTROLLED OXYGEN SATURATION

Номер: US20140080186A1
Автор: Dassler Tobias, Reutter-Maier Anneliese, SCHLOESSER Thomas
Принадлежит: Wacker Chemie AG

The invention relates to a method for producing L-cystine by fermenting a microorganism strain in a fermentation medium, in which method L-cystine is precipitated in an amount of at least 70% relative to the total cysteine, characterized in that the Osaturation of the fermentation medium is kept at least at 1% and at most at 40±3% during the formation of L-cystine. 1. A method for producing L-cystine comprising fermenting a microorganism strain in a fermentation medium , wherein the L-cystine precipitates in an amount of at least 70% relative to total amount of cysteine , and are Osaturation of the fermentation medium during L-cystine production is maintained at least at 1% and at most at 40±3%.2. The method as claimed in claim 1 , wherein the Osaturation during the formation of L-cystine is maintained below 30±3%.3. The method as claimed in claim 1 , wherein the microorganism strain used is a representative from the Enterobacteriaceae family.4. The method as claimed in claim 3 , wherein (a) the microorganism strain either has a serine O-acetyltransferase claim 3 , which has a feedback inhibition by L-cysteine reduced by at least a factor of 2 in comparison to a corresponding wild type enzyme claim 3 , or (b) the microorganism strain has a cysteine export increased by at least a factor of 2 by overexpression of an efflux gene in comparison to a wild type strain.5. The method as claimed in claim 4 , wherein the microorganism strain additionally has a 3-phosphoglycerate dehydrogenase having a feedback inhibition by L-serine reduced by at least a factor of 2 in comparison to the corresponding wild type enzyme.6. The method as claimed in claim 1 , wherein oxygen is introduced into the fermentation medium by shaking the culture vessel by use of a shaking device or by blowing in air or pure oxygen or a mixture of these gases.7. The method as claimed in claim 1 , wherein a carbon source is added to the fermentation medium such that a level of the carbon source in a ...

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Номер записи: 72
20-03-2014 дата публикации

SERINOL PRODUCTION IN GLYCEROL CATABOLISM DEFICIENT ESCHERICHIA COLI STRAINS

Номер: US20140080187A1
Автор: Andreessen Bjoern, MAKSYM Lukas, Steinbuechel Alexander
Принадлежит:

The invention is about host cells which are capable to convert glycerol to serinol. Furthermore, a process for producing serinol is disclosed, which comprises culturing host cells inactive for triosephosphate isomerase and active for dihydroxyacetone phosphate aminotransferase to convert glycerol to serinol, induction of conversion from glycerol to serinol by adding at least glycerol to the cell culture, and isolating serinol from the cell culture. 1. A process for producing serinol , which comprises{'i': 'E. coli', 'i) culturing host cells inactive for triosephosphate isomerase and active for dihydroxyacetone phosphate aminotransferase to convert glycerol to serinol,'}ii) induction of conversion from glycerol to serinol by adding at least glycerol to the cell culture, andiii) isolating serinol from the cell culture.2E. coli. The process according to claim 1 , wherein the host cells are in addition inactive for methylglyoxal synthase.3E. coli. The process according to claim 1 , wherein glp DNA-binding transcriptional repressor is inactivated additionally in the host cells.4. The process according to claim 1 , wherein expression of active dihydroxyacetone phosphate aminotransferase is achieved by introducing an expression vector into the host cells comprising the transgene coding for dihydroxyacetone phosphate aminotransferase which is active for conversion of glycerol to serinol.5. An isolated recombinant expression vector comprising transgene coding for dihydroxyacetone phosphate aminotransferase which is active for conversion of glycerol to serinol and wherein the expression of the dihydroxyacetone phosphate aminotransferase is inducible.6. The isolated recombinant expression vector according to claim 4 , wherein the vector is pCOLADuet-1.8E. coliE. coli. A recombinant strain active for dihydroxyacetone phosphate aminotransferase capable to convert glycerol to serinol claim 4 , wherein triosephosphate isomerase is inactivated in the host cells.9E. coliE. coli. The ...

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Номер записи: 73
27-03-2014 дата публикации

METHOD FOR PRODUCING AQUEOUS ACRYLAMIDE SOLUTION

Номер: US20140087434A1
Автор: Hagiya Norifumi, Kanou Makoto
Принадлежит: MITSUBISHI RAYON CO., LTD.

There is provided a method for producing an aqueous acrylamide solution by reacting a composition including acrylonitrile with water to produce acrylamide, in which the composition including acrylonitrile includes 3 to 15 mg of propionitrile per 1 kg of the total weight of the composition including acrylonitrile. According to the present invention, a production method with which it is possible to suppress acrylamide polymerization without lowering quality and thereby obtain a stable aqueous acrylamide solution can be provided. 1. A method for producing an aqueous acrylamide solution , the method comprising reacting a composition comprising acrylonitrile and water to produce acrylamide , wherein the composition further comprises 3 to 15 mg of propionitrile per 1 kg of the total weight of the composition.2. The method according to claim 1 , wherein the reacting occurs in the presence of a biocatalyst.3. The method according to claim 1 , wherein the composition further comprises 2 to 20 mg/kg of acetonitrile per 1 kg of the total weight of the composition.4. The method according to claim 1 , wherein a concentration of the acrylamide in the aqueous acrylamide solution is 30 to 60% by mass relative to the total mass of the aqueous acrylamide solution.5. The method according to claim 2 , wherein the composition further comprises 2 to 20 mg/kg of acetonitrile per 1 kg of the total weight of the composition.6. The method according to claim 2 , wherein a concentration of the acrylamide in the aqueous acrylamide solution is 30 to 60% by mass relative to the total mass of the aqueous acrylamide solution.7. The method according to claim 3 , wherein a concentration of the acrylamide in the aqueous acrylamide solution is 30 to 60% by mass relative to the total mass of the aqueous acrylamide solution. The present invention relates to a method for producing an aqueous acrylamide solution.The present application claims priority to Japanese Patent Application No. 2011-112428, which ...

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Номер записи: 74
10-04-2014 дата публикации

MICROORGANISMS AND METHODS FOR PRODUCING ACRYLATE AND OTHER PRODUCTS FROM HOMOSERINE

Номер: US20140099676A1
Автор: Green Phillip Richard, Saunders Charles Winston, Velásquez Juan Esteban, Xu Jun
Принадлежит:

This invention relates to microorganisms that convert a carbon source to acrylate or other desirable products using homoserine and 2-keto-4-hydroxybutyrate as intermediates. The invention provides genetically engineered microorganisms that carry out the conversion, as well as methods for producing acrylate by culturing the microorganisms. Also provided are microorganisms and methods for converting homoserine to 3-hydroxypropionyl-CoA, 3-hydroxypropionate (3HP), poly-3-hydroxypropionate and 1,3-propanediol. 1. A method for converting homoserine to 3-hydroxypropionyl-CoA comprising the steps of:{'smallcaps': L', 'L, 'a) converting homoserine to 2-keto-4-hydroxybutyrate, wherein this conversion is catalyzed by at least one enzyme selected from the group consisting of an aminotransferase, an -amino acid oxidase and an -amino acid dehydrogenase; and'}b) converting 2-keto-4-hydroxybutyrate to 3-hydroxypropionyl-CoA, wherein this conversion is catalyzed by at least one enzyme selected from the group consisting of a 2-ketoacid dehydrogenase and a combination of a 2-ketoacid decarboxylase and a dehydrogenase.2. The method of in which a recombinant microorganism overexpresses one or more genes to convert homoserine to 3-hydroxypropionyl-CoA.3. The method of in which the microorganism expresses a poly-3-hydroxyalkanoate synthase to further convert 3-hydroxypropionyl-CoA to a poly-3-hydroxyalkanoate containing 3-hydroxypropionate monomers.4. The method of further comprising the steps of:c) converting 3-hydroxypropionyl-CoA to acryloyl-CoA, wherein this conversion is catalyzed by a dehydratase; andd) converting acryloyl-CoA to acrylic acid, wherein this conversion is catalyzed by at least one enzyme selected from the group consisting of a thioesterase, a CoA-transferase, and a combination of a phosphate transferase and kinase.5. The method of in which a recombinant microorganism converts homoserine to acrylic acid.6. The method of in which 3-hydroxypropionyl-CoA is further ...

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Номер записи: 75
10-04-2014 дата публикации

CORYNEBACTERIUM SP. TRANSFORMED WITH A FRUCTOKINASE GENE DERIVED FROM ESCHERICHIA SP. AND PROCESS FOR PREPARING L-AMINO ACID USING THE SAME

Номер: US20140099680A1
Автор: BAE Hyun Ae, Bae Hyun Won, Jang Jae Woo, KIM Dae Cheol, KIM Hyo Jin, Kim Hyung Joon, KIM Jong Chul, Kim Tae Han, Lee Kyung Han, Lim Sang Jo, Moon Jun Ok, Sung Jin Suck
Принадлежит: CJ CHEILJEDANG CORPORATION

The present invention relates to sp. that is transformed with an sp.-derived fructokinase gene to express fructokinase showing a sufficient activity of converting fructose into fructose-6-phosphate, thereby preventing unnecessary energy consumption, and a method for producing L-amino acids using the strain. The transformed sp. of the present invention is able to express fructokinase from the -derived fructokinase gene to prevent unnecessary energy consumption during fructose metabolism, leading to more cost-effective production of L-amino acids. Therefore, it can be widely used for the effective production of L-amino acids. 1CorynebacteriumEscherichia. sp. for producing L-amino acids , comprising an sp.-derived fructokinase gene operably linked to a gene expression unit.2Corynebacterium. The sp. for producing L-amino acids according to claim 1 , wherein the fructokinase gene is cscK or mak.3Corynebacterium. The sp. for producing L-amino acids according to claim 1 , wherein the fructokinase gene has a nucleotide sequence of SEQ ID NO. 17 or SEQ ID NO. 18.4CorynebacteriumCorynebacteriumCorynebacterium. The sp. for producing L-amino acids according to claim 1 , wherein the gene expression unit is operably linked to a vector claim 1 , and included in microorganism by transformation or included by insertion into the chromosome of microorganism.5Corynebacterium. The sp. for producing L-amino acids according to claim 1 , wherein the gene is overexpressed by modification of gene expression regulatory region.6Corynebacterium. The sp. for producing L-amino acids according to claim 5 , wherein the regulatory region is promoter which is selected from the group consisting of a cscK promoter claim 5 , a mak promoter claim 5 , a pcj7 promoter claim 5 , a lysCP1 promoter claim 5 , an EF-Tu promoter claim 5 , a groEL promoter and an aceAB promoter.7Corynebacterium. The sp. for producing L-amino acids according to claim 1 , wherein the L-amino acid is L-lysine claim 1 , L-threonine ...

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Номер записи: 76
10-04-2014 дата публикации

Enzymatic Synthesis of Optically Active Chiral Amines

Номер: US20140099682A1
Автор: JOSHI Sunil Vaman, Swaminathan Arumugam Govind
Принадлежит: EMBIO LIMITED

The present invention relates to method of production of optically active chiral amine from alpha hydroxy ketone using enzyme transaminase as the biocatalyst. In particular the present invention relates to production of (1R, 2S)-Norephedrine and its salts from R-Phenylacetylcarbinol (R-PAC) by employing S-transaminase as the biocatalyst and Isopropylamine as the amine donor. 1. A process for producing optically active chiral amine comprising:a. providing an amino acceptor or keto substrate selected from a series of alpha hydroxy ketone and an amino donor;b. reacting the keto substrate and the amino donor with a (R) or (S)-selective transaminase; andc. finally obtaining the desired optically active chiral amine and a ketone by-product; wherein the process is carried out in a reaction mixture having a pH from approximately 6-8 for a reaction time of 12-48 hours in a temperature range from (25-35° C.)2. The process according to claim 1 , wherein the alpha hydroxy ketone is R-phenylacetylcarbinol.3. The process according to claim 1 , wherein the amino donor is selected from a group including amines or amino acids claim 1 , in particular from isopropylamine (also termed 2-aminopropane) claim 1 , α-phenylethylamine (also termed 1-phenylethanamine) claim 1 , and its enantiomers (S)-1-phenylethanamine and (R)-1-phenylethanamine claim 1 , 2-amino-4-phenylbutane claim 1 , glycine claim 1 , L-glutamic acid claim 1 , L-glutamate claim 1 , monosodium glutamate claim 1 , L-alanine claim 1 , D-alanine claim 1 , D claim 1 ,L-alanine claim 1 , L-aspartic acid claim 1 , L-lysine claim 1 , L-ornithine claim 1 , β-alanine claim 1 , taurine claim 1 , n-octylamine claim 1 , cyclohexylamine claim 1 , 1 claim 1 ,4-butanediamine claim 1 , 1 claim 1 ,6-hexanediamine claim 1 , 6-aminohexanoic acid claim 1 , 4-aminobutyric acid claim 1 , tyramine claim 1 , and benzyl amine claim 1 , 2-aminobutane claim 1 , 2-amino-1-butanol claim 1 , 1-amino-1-(2-methoxy-5-fluorophenyl)ethane claim 1 , 1-amino ...

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Номер записи: 77
05-01-2017 дата публикации

E-POLYLYSINE HYDROGEL AND PREPARATION METHOD AND APPLICATION THEREOF

Номер: US20170000924A1
Автор: Chi Bo, Feng Xiaohai, Li Sha, Liang Jinfeng, OUYANG Pingkai, Wang Rui, Xu Hong
Принадлежит: NANJING TECH UNIVERSITY

The present invention discloses a ε-polylysine hydrogel and the preparation method and application of the as-described ε-polylysine hydrogel. The polylysine hydrogel is non-toxic to a recipient, and has biodegradability and biocompatibility. The wound tissue healing material prepared by the present invention can be used in wound tissue adhesion in an efficient, stable, safe manner. 2. A process for preparing the ε-polylysine hydrogel as described in claim 1 , comprises the following steps:(1) adding a polyethylene glycol into dichlormethane, adding 4-dimethylaminopyridine and triethylamine reacting for 20-150 min at room temperature; then adding dropwisely the reaction mixture into a solution of p-nitrophenylchloroformate in dichlormethane under inert gas shielding condition at room temperature, reacting for 12 to 72 hours; evaporating and then adding dropwisely into a cold diethyl ether solution; removing precipitates from mixed solution by filtration and vacuum freeze-drying to obtain a p-nitrophenylchloroformate-polyethylene glycol-p-nitrophenylchloroformate copolymer;(2) dissolving the p-nitrophenylchloroformate-polyethylene glycol-p-nitrophenylchloroformate copolymer into a phosphate buffer; then adding a tyramine dissolved in the phosphate buffer, reacting for 5 to 72 hours at room temperature to obtain a solution of p-nitrophenylchloroformate-polyethylene glycol-tyramine copolymer;(3) dissolving a ε-polylysine into the phosphate buffer, then adding the p-nitrophenylchloroformate-polyethylene glycol-tyramine copolymer solution from step (2), and reacting at room temperature for 12 to 72 hours; removing the p-nitrophenylchloroformate precipitate by filtration, following by dialyzing the filtrate in purified water for 4 to 8 days; freeze-drying the filtrate to obtain a E-polylysine grafted with polyethylene glycol and tyramine;(4) dissolving the ε-polylysine-polyethylene glycol-tyramine from step (3) into the water or phosphate buffer; adding a mixed aqueous ...

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Номер записи: 78
07-01-2016 дата публикации

IN VIVO AND IN VITRO OLEFIN CYCLOPROPANATION CATALYZED BY HEME ENZYMES

Номер: US20160002682A1
Автор: Arnold Frances H., Brustad Eric M., Coelho Pedro S., Lewis Jared C., Wang Zhan
Принадлежит:

The present invention provides methods for catalyzing the conversion of an olefin to any compound containing one or more cyclopropane functional groups using heme enzymes. In certain aspects, the present invention provides a method for producing a cyclopropanation product comprising providing an olefinic substrate, a diazo reagent, and a heme enzyme; and admixing the components in a reaction for a time sufficient to produce a cyclopropanation product. In other aspects, the present invention provides heme enzymes including variants and fragments thereof that are capable of carrying out in vivo and in vitro olefin cyclopropanation reactions. Expression vectors and host cells expressing the heme enzymes are also provided by the present invention. 182-. (canceled)84. The reaction mixture of claim 83 , wherein each Rand Ris independently an optionally substituted Calkyl.85. The reaction mixture of claim 83 , wherein each Ris independently an optionally substituted Calkyl.86. The reaction mixture of claim 83 , wherein Ris a phenyl group.87. The reaction mixture of claim 83 , wherein the carbene precursor is a diazo reagent selected from the group consisting of diazomethane claim 83 , an α-diazoester claim 83 , an α-diazoamide claim 83 , an α-diazonitrile claim 83 , an α-diazoketone claim 83 , and an α-diazoaldehyde.89. The reaction mixture of claim 87 , wherein the diazo reagent is ethyl diazoacetate.90. The reaction mixture of claim 83 , wherein the olefinic substrate and the carbene precursor are part of the same substrate.91. The reaction mixture of claim 83 , wherein the cyclopropanation product is produced in vitro.92. The reaction mixture of claim 83 , wherein the reaction mixture further comprises a reducing agent.93. The reaction mixture of claim 83 , wherein the heme enzyme is localized within a whole cell and the cyclopropanation product is produced in vivo.94. The reaction mixture of claim 83 , wherein the cyclopropanation product is produced under anaerobic ...

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Номер записи: 79
07-01-2016 дата публикации

Polypeptides Having Peroxygenase Activity and Polynucleotides Encoding Same

Номер: US20160002683A1
Автор: Lars Henrik Oestergaard, Lisbeth Kalum, Sara Landvik
Принадлежит: Novozymes AS

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.

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Номер записи: 80
07-01-2016 дата публикации

Method for Producing L-Lysine by Modifying Aconitase Gene and/or Regulatory Elements thereof

Номер: US20160002684A1
Автор: CHEN Jinlong, Guo Xiaowei, LIANG Yong, LIU Shuwen, MA Jiyin, MENG Gang, REN Rui, SHANG Xiuling, WEI Aiying, WEN Tingyi, YANG Lipeng, Zhang Yun, ZHAO Chunguang
Принадлежит:

A method for producing L-lysine by fermentation comprises the steps of modifying an aconitase gene and/or regulatory element thereof in a chromosome of a bacterium so that the activity and/or the expression amount of the aconitase of the bacterium are reduced but not eliminated; and producing L-lysine by the fermentation of the modified bacterium. In addition, also provided are methods and uses derived from the method as well as bacteria used in these methods and uses. 1. A method of producing L-lysine by fermentation or of increasing a fermentation yield of L-lysine , which comprises the steps of:(1) modifying an aconitase gene and/or regulatory element thereof in a chromosome of a bacterium so that the activity and/or the expression amount of the aconitase of the bacterium are reduced but not eliminated; and(2) producing L-lysine by fermentation with the bacterium obtained by the modification of step (1).2. A use of a bacterium obtained by a modification for producing L-lysine by fermentation or for increasing a fermentation yield of L-lysine , wherein the modification is to modify an aconitase gene and/or regulatory element thereof in a chromosome of a bacterium , and the activity and/or the expression amount of the aconitase of the bacterium obtained by the modification are reduced but not eliminated.3. The method according to claim 1 , which comprises the step of modifying an aconitase gene and/or regulatory element thereof in a chromosome of a bacterium so that the activity and/or the expression amount of the aconitase of the bacterium obtained by the modification are reduced but not eliminated.43. The method according to claim 1 , wherein the step of modifying an aconitase gene in a chromosome of a bacterium is an addition claim 1 , deletion or substitution of one or more nucleotides in the nucleotide sequence of the aconitase gene.5. The method according to claim 4 , wherein the substitution includes a substitution for the initiation codon of the aconitase ...

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Номер записи: 81
07-01-2016 дата публикации

ENGINEERED TRANSAMINASE POLYPEPTIDES FOR INDUSTRIAL BIOCATALYSIS

Номер: US20160002688A1
Автор: Eberhard Ellen, NAZOR Jovana, Quintanar-Audelo Martina, SMITH Derek, Wang Cuixia
Принадлежит:

The present disclosure provides engineered transaminase polypeptides useful for the synthesis of chiral amine compounds under industrially relevant conditions. The disclosure also provides polynucleotides encoding the engineered transaminase polypeptides, host cells capable of expressing the engineered transaminases, and methods of using the engineered transaminases for the production of chiral amine compounds. 1. An engineered polypeptide having transaminase activity comprising an amino acid sequence having at least 80% sequence identity to reference sequence of SEQ ID NO:2 and(a) an amino acid residue difference as compared to SEQ ID NO:2 selected from X33L, X36C, X41C/F/K/M/N/R, X42, X48D/E/G/K/T, X51K, X54, X76S, X122F/Q, X148Q, X152T, X155A/I/K/T/V, X156R, X160P, X215G/H/L, X241R, X270T, X273H, X325M and X241R; or(b) a combination of residue differences selected from: X42G, X54P, X152S, and X155T; X42G, X54P, X152S, X155T, and R164P; X42G, X54P, X150F, X152S, and X155T; X42G, X54P, X150F, X152S, X155T, and X267V; X42G, X54P, X150F, X152S, X155L, W156Q, and C215G; X42G, X54P, X150F, X152S, X155T, X215G, and X267V; X33L; X42G, X54P, X117G; X150F, X152S, X155I, X156Q, and C215G; X41K, X42G, X54P, X150F, X152S, X155K, X156Q, and C215G; X33L, X42G, X54P, X109S, X150F, X152S, X155K, X156Q, and X215H; X33L, X42G, X54P, X150F, X152S, X155I, X156Q, and X215G; X33L, X42G, X54P, X150F, X152S, X155K, X156Q, and X215H; X33L, X42G, X54P, X150F, X152S, X155L, X156Q, and X215H; X33L, X42G, X54P, X150F, X152S, X155L, X156Q, X215H, and X241R; X41F, X42G, X54P, X122Q, X150F, X152T, X155V, X156Q, and X215G; X41F, X42G, X54P, X150F, X152S, X155L, X156Q, X171I, X215G, and X241R; X41F, X42G, X54P, X150F, X152S, X155I, X156Q, V171I, and X215G; X41F, X42G, X54P, X150F, X152S, X155I, X156Q, and X215G; X41F, X42G, X54P, X150F, X152S, X155L, X156Q, X171I, and X215G; X41F, X42G, X54P, X150F, X152S, X155L, X156Q, and X215G; X42G, X48G, X54P, X150F, X152S, X155L, X156Q, and X215H; X42G, X54P ...

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Номер записи: 82
05-01-2017 дата публикации

OMEGA-TRANSAMINASE OF R CONFIGURATION AND USES THEREOF

Номер: US20170002338A1
Автор: Gao Feng, HONG Hao, LI Shaohe, LI Yanjun, Zhang Yan
Принадлежит:

An omega-transaminase of R-configuration is provided. The omega-transaminase of R-configuration has the amino acid sequence as shown in SEQ ID NO: 2, or has at least 80% identity to the amino acid sequence as shown in SEQ ID NO: 2, or has the amino acid sequence of proteins which have substituted, deleted or added one or more amino acids and have the activity of an omega-transaminase with a high stereoselectivity R-configuration catalytic activity; and does not have the amino acid sequence encoded by the nucleotide sequence as shown in SEQ ID NO: 4. The high stereoselectivity refers to the content of one of the stereoisomers being at least about 1.1 times that of the other. A use of the omega-transaminase of R-configuration is provided. 1. An omega-transaminase of R-configuration or a modified compound , functional equivalent , functional fragment or variant thereof , wherein an amino acid sequence of the omega-transaminase of R-configuration comprises a sequence selected from one of the following sequences:a) an amino acid sequence as shown in SEQ ID NO: 2;b) an amino acid sequence with at least 80% identity to the amino acid sequence as shown in SEQ ID NO: 2 and having the activity of an omega-transaminase with high stereoselective R-configuration catalytic activity, wherein the amino acid sequence is not an amino acid sequence encoded by a nucleotide sequence as shown in SEQ ID NO: 4; andc) a protein derived from SEQ ID NO: 2 by subjecting the amino acid sequence as shown in SEQ ID NO: 2 to substitution, deletion or addition one or more amino acids, and having the activity of an omega-transaminase with high stereoselective R-configuration catalytic activity, wherein the amino acid sequence is not the amino acid sequence encoded by the nucleotide sequence as shown in SEQ ID NO: 4, andwherein the high stereoselective refers to the content of one of the stereoisomers being at least about 1.1 times that of the other.2. The transaminase according to claim 1 , wherein ...

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Номер записи: 83
05-01-2017 дата публикации

Recombinant Microorganisms of Escherichia with L-threonine Productivity and Method of Producing L-threonine Using the Same

Номер: US20170002365A1
Автор: HONG Hyeong Pyo, Hwang Young Bin, Kim Hyung Joon, KOH Eun Sung, KWON Su Yon, LEE Ji Sun, LEE Keun Cheol
Принадлежит: CJ CHEILJEDANG CORPORATION

The present invention relates to an mutant strain having enhanced L-threonine productivity, which is obtained by introducing the permease of origin, and to method of producing L-threonine using the mutant strain. 1EscherichiaCorynebacterium. A recombinant microorganism of the genus having enhanced L-threonine productivity , wherein the recombinant microorganism is obtained by transformation so as to contain permease of origin represented by SEQ ID NO: 1 or SEQ ID NO: 2.2EscherichiaEscherichia coli.. The recombinant microorganism of the genus having enhanced L-threonine productivity claim 1 , according to claim 1 , wherein the recombinant microorganism is3EscherichiaCorynebacterium. The recombinant microorganism of the genus according to claim 1 , wherein the recombinant microorganism is obtained by transformation so as to contain both the permeases of SEQ ID NO: 1 and SEQ ID NO: 2.4EscherichiaEscherichia coli.. The recombinant microorganism of the genus according to claim 1 , wherein the microorganism is5. A method for producing L-threonine claim 1 , comprising the steps of:{'claim-ref': {'@idref': 'CLM-00001', 'claim 1'}, 'inoculating and culturing the microorganism of ; and'}separating L-amino acid from the culture.6. A method for producing L-threonine claim 1 , comprising the steps of:{'claim-ref': {'@idref': 'CLM-00002', 'claim 2'}, 'inoculating and culturing the microorganism of ; and'}separating L-amino acid from the culture.7. A method for producing L-threonine claim 1 , comprising the steps of:{'claim-ref': {'@idref': 'CLM-00003', 'claim 3'}, 'inoculating and culturing the microorganism of ; and'}separating L-amino acid from the culture. The present invention relates to a recombinant microorganism of the genus having enhanced L-threonine productivity, which is obtained by modifying a microorganism of the genus so as to express the permease of origin, and to a method of producing L-threonine using the recombinant microorganism.L-threonine, a kind of essential ...

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Номер записи: 84
05-01-2017 дата публикации

PROCESSES FOR FERMENTATION OF LIGNOCELLULOSIC GLUCOSE TO ALIPHATIC ALCOHOLS OR ACIDS

Номер: US20170002387A1
Автор: PYLKKANEN Vesa, RETSINA Theodora
Принадлежит:

A process for producing an organic aliphatic product (such as butanol) from lignocellulosic biomass is provided, comprising: (a) fractionating lignocellulosic biomass in the presence of a solvent for lignin, a hydrolysis catalyst, and water, to produce a liquor containing hemicellulose, cellulose-rich solids, and lignin; (b) washing the cellulose-rich solids and separating the cellulose-rich solids from the liquor; (c) enzymatically hydrolyzing the cellulose-rich solids to generate a hydrolysate comprising glucose; (d) detoxifying the hydrolysate by neutralizing the hydrolysate, removing insoluble solids, and removing or oxidizing residual hydrolysis catalyst, thereby generating a purified hydrolysate; (e) fermenting the purified hydrolysate using a suitable microorganism to produce a dilute organic aliphatic product, wherein the microorganism is recycled with a membrane; (f) extracting the dilute organic aliphatic product into a water-immiscible extractant, to generate an intermediate material; and (g) distilling the intermediate material to generate a concentrated organic aliphatic product. 1. A process for producing an organic aliphatic product from lignocellulosic biomass , said process comprising:(a) fractionating a feedstock comprising lignocellulosic biomass in the presence of a solvent for lignin, a hydrolysis catalyst, and water, to produce a liquor containing hemicellulose, cellulose-rich solids, and lignin;(b) washing said cellulose-rich solids and separating said cellulose-rich solids from said liquor;(c) enzymatically hydrolyzing said cellulose-rich solids to generate a hydrolysate comprising glucose;(d) detoxifying said hydrolysate by neutralizing said hydrolysate, removing insoluble solids, and removing or oxidizing residual hydrolysis catalyst, thereby generating a purified hydrolysate;(e) fermenting said purified hydrolysate using a suitable microorganism in a fermentor to produce a dilute organic aliphatic product, wherein said microorganism is ...

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Номер записи: 85
05-01-2017 дата публикации

MICROORGANISMS HAVING ENHANCED L-AMINO ACIDS PRODUCTIVITY AND PROCESS FOR PRODUCING L-AMINO ACIDS USING THE SAME

Номер: US20170002388A1
Автор: HONG Hyeong Pyo, JANG Juno, KOH Eun Sung, KWON Su Yon, LEE Ji Sun, LEE Keun Cheol, Lee Kwang Ho
Принадлежит:

Disclosed are a recombinant microorganism having enhanced L-amino acid productivity, wherein the recombinant microorganism is transformed to have removed or decreased activity of at least one of adenosine deaminase and AMP nucleosidase, and a method of producing an L-amino acid using the recombinant microorganism. The use of the recombinant microorganism may enable the production of the L-amino acid in a highly efficient manner. 1. A recombinant microorganism having enhanced producibility of an L-amino acid , wherein activity of at least one of adenosine deaminase comprising an amino acid sequence of SEQ ID NO: 14 and AMP nucleosidase comprising an amino acid sequence of SEQ ID NO: 16 removed or decreased.2. The recombinant microorganism of claim 1 , wherein the L-amino acid is L-threonine or L-tryptophan.3Escherichia.. The recombinant microorganism of claim 1 , the recombinant microorganism belongs to the genus4Escherichia coli.. The recombinant microorganism of claim 3 , wherein the recombinant microorganism is5. A method of producing L-amino acid claim 3 , the method comprising:{'claim-ref': {'@idref': 'CLM-00001', 'claim 1'}, 'culturing the recombinant microorganism of ; and'}collecting an L-amino acid from the culture.6. The method of claim 5 , wherein the L-amino acid is L-threonine or L-tryptophan.7. A method of producing L-amino acid claim 5 , the method comprising:{'claim-ref': {'@idref': 'CLM-00002', 'claim 2'}, 'culturing the recombinant microorganism of ; and'}collecting an L-amino acid from the culture.8. A method of producing L-amino acid claim 5 , the method comprising:{'claim-ref': {'@idref': 'CLM-00003', 'claim 3'}, 'culturing the recombinant microorganism of ; and'}collecting an L-amino acid from the culture.9. A method of producing L-amino acid claim 5 , the method comprising:{'claim-ref': {'@idref': 'CLM-00004', 'claim 4'}, 'culturing the recombinant microorganism of ; and'}collecting an L-amino acid from the culture. The present invention ...

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Номер записи: 86
04-01-2018 дата публикации

IMMOBILIZED CELL AND PREPARATION METHOD THEREOF

Номер: US20180002686A1
Автор: Li Naiqiang, Liu Charlie, LIU Xiucai, Yu Lijun
Принадлежит:

Provided are a lysine decarboxylase immobilized cell and preparation method thereof. 2. The method of immobilizing cells containing lysine decarboxylase according to claim 1 , wherein the resulting solution further comprises one or more of a natural macromolecule material and a second synthetic macromolecule material claim 1 , or a mixture thereof claim 1 , wherein the natural macromolecule material and the second synthetic macromolecule material are natural or synthetic macromolecule material having a gel-forming ability claim 1 , and the second synthetic macromolecule material is different from the first synthetic macromolecule material.3. The method of immobilizing cells containing lysine decarboxylase according to claim 2 , wherein the first synthetic macromolecule material claim 2 , the second synthetic macromolecule material are one or more selected from the group consisting of polyvinyl alcohol claim 2 , polyethylene glycol claim 2 , polyacrylonitrile claim 2 , acetate fibers claim 2 , and diacetate fibers claim 2 , preferably selected from the group consisting of polyvinyl alcohol and polyethylene glycol.4. The method of immobilizing cells containing lysine decarboxylase according to claim 2 , wherein the natural macromolecule material is one or more selected from the group consisting of sodium alginate claim 2 , carrageenan claim 2 , xanthan gum claim 2 , activated carbon claim 2 , diatomaceous earth claim 2 , curdlan claim 2 , and chitosan claim 2 , preferably sodium alginate.5. The method of immobilizing cells containing lysine decarboxylase according to claim 2 , wherein the resulting solution is a mixed solution of polyvinyl alcohol and sodium alginate or a mixed solution of polyvinyl alcohol and polyethylene glycol claim 2 , preferably claim 2 , the addition amount of the polyvinyl alcohol is 1 to 13 wt % claim 2 , the addition amount of sodium alginate is 0.1 to 3 wt % claim 2 , and the addition amount of the polyethylene glycol is 0.1 to 5 wt %.6. ...

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Номер записи: 87
02-01-2020 дата публикации

MICROORGANISMS FOR PRODUCING PUTRESCINE OR ORNITHINE AND PROCESS FOR PRODUCING PUTRESCINE OR ORNITHINE USING THEM

Номер: US20200002686A1
Автор: JUNG Hee Kyoung, LEE Baek Seok, LEE Hyo Hyoung, Lee Kyoung Min, LI Hong Xian, Park Su Jin, Um Hye Won, YANG Young Lyeol
Принадлежит:

Disclosed is a modified microorganism producing putrescine or ornithine, and a method for producing putrescine or ornithine using the same. 115-. (canceled)16. A method for producing putrescine or ornithine , comprising:{'i': Corynebacterium', 'E. coli', 'E. coli, '(i) culturing a modified microorganism of the genus producing putrescine or ornithine in a medium, wherein activities of N-acetylglutamate synthase from and acetylornithine deacetylase from are introduced into the microorganism; and'}(ii) recovering putrescine or ornithine from the cultured microorganism or the medium.17CorynebacteriumCorynebacterium glutamicum.. The method according to claim 16 , wherein the microorganism of the genus is18E. coliE. coli. The method according to claim 16 , wherein the N-acetylglutamate synthase from consists of an amino acid sequence of SEQ ID NO: 1 claim 16 , and/or the acetylornithine deacetylase from consists of an amino acid sequence of SEQ ID NO: 3.19. The method according to claim 16 , wherein (a) an activity of phosphotransacetylase and acetate kinase operon (pta-ackA operon); (b) an activity of at least one selected from the group consisting of acetyl gamma glutamyl phosphate reductase (ArgC) claim 16 , acetylglutamate synthase or ornithine acetyltransferase (ArgJ) claim 16 , acetylglutamate kinase (ArgB) claim 16 , and acetyl ornithine aminotransferase (ArgD); and/or (c) an activity of putrescine exporter is further enhanced compared to its endogenous activity.20E. coli. The method according to claim 16 , wherein an activity of acetyl-CoA synthetase (acs) from claim 16 , and/or an activity of ornithine decarboxylase (ODC) is further introduced.21. The method according to claim 16 , wherein (a) an activity of i) ornithine carbamoyltransferase (ArgF) claim 16 , ii) glutamate exporter claim 16 , or iii) ornithine carbamoyltransferase and glutamate exporter and/or (b) an activity of acetyltransferase is further weakened compared to its endogenous activity. This ...

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Номер записи: 88
02-01-2020 дата публикации

PUTRESCINE-PRODUCING MICROORGANISM AND METHOD FOR PRODUCING PUTRESCINE USING THE SAME

Номер: US20200002737A1
Автор: Lee Jae Hun, LEE Na Hum, LI Hong Xian, Moon Jun Ok, Um Hye Won
Принадлежит: CJ CHEILJEDANG CORPORATION

The present application relates to a putrescine-producing microorganism in which the activity of formate dehydrogenase is increased, and a method for producing putrescine using the same. 1Corynebacterium. A putrescine-producing microorganism of the genus , in which the activity of formate dehydrogenase (Fdh) is increased compared to that before modification.2Candida boidinii.. The microorganism according to claim 1 , wherein the Fdh is derived from3. The microorganism according to claim 1 , wherein the Fdh consists of the amino acid sequence of SEQ ID NO: 10.4. The microorganism according to claim 1 , wherein the activity of ornithine decarboxylase (ODC) is further introduced.5. The microorganism according to claim 1 , wherein the activity of acetyltransferase is further weakened compared to its endogenous activity.6. The microorganism according to claim 1 , wherein the activity of the protein that exhibits the activity of exporting putrescine is increased compared to its endogenous activity.7Corynebacterium glutamicum.. The microorganism according to claim 1 , wherein the microorganism is8. A method of producing putrescine claim 1 , comprising:{'claim-ref': {'@idref': 'CLM-00001', 'claim 1'}, '(a) culturing the microorganism of in a medium; and'}(b) recovering putrescine from the microorganism or the cultured medium obtained in step (a).9. The method according to claim 8 , wherein the microorganism is cultured in a medium not containing formic acid.10. The method according to claim 8 , wherein the microorganism is cultured under an aerobic condition.11. A method of producing putrescine claim 2 , comprising: (a) culturing the microorganism of in a medium; and (b) recovering putrescine from the microorganism or the cultured medium obtained in step (a).12. A method of producing putrescine claim 3 , comprising: (a) culturing the microorganism of in a medium; and (b) recovering putrescine from the microorganism or the cultured medium obtained in step (a).13. A method of ...

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Номер записи: 89
07-01-2021 дата публикации

BIOCATALYSTS AND METHODS FOR THE SYNTHESIS OF ARMODAFINIL

Номер: US20210002618A1
Автор: ALVIZO Oscar, Ang Ee Lui, Behrouzian Behnaz, Clay Michael D., Collier Steven J., Eberhard Ellen D., Fan Fu, Smith Derek J., Song Shiwei, Widegren Magnus, Wilson Robert, Xu Junye, ZHU Jun
Принадлежит:

The present invention relates to non-naturally occurring polypeptides useful for preparing armodafinil, polynucleotides encoding the polypeptides, and methods of using the polypeptides. The non-naturally occurring polypeptides of the present invention are effective in carrying out biocatalytic conversion of the (i) 2-(benzhydrylsulfinyl)acetamide to (−)-2-[(R)-(diphenylmethyl)sulfinyl]acetamide (armodafinil), or (ii) benzhydryl-thioacetic acid to (R)-2-(benzhydrylsulfinyl)acetic acid, which is a pivotal intermediate in the synthesis of armodafinil, in enantiomeric excess. 1. A non-naturally occurring polynucleotide encoding a non-naturally occurring polypeptide having cyclohexanone monooxygenase (CHMO) activity wherein the amino acid sequence of the polypeptide has at least 90% sequence identity to SEQ ID NO: 136 , and one or more amino acid substitutions compared to the naturally occurring polypeptide at one or more positions corresponding to positions in SEQ ID NO: 136 , selected from the group consisting of 75 , 79 , 82 , 99 , 110 , 166 , 172 , 208 , 216 , 273 , 324 , 364 , 395 , 412 , 491 , 503 , and 504.3. The non-naturally occurring polynucleotide encoding the non-naturally occurring polypeptide of claim 1 , wherein said non-naturally occurring polypeptide further comprises one or more amino acid substitutions relative to SEQ ID NO: 136 claim 1 , wherein the polypeptide comprises an alanine claim 1 , glutamic acid claim 1 , glycine claim 1 , isoleucine claim 1 , lysine claim 1 , proline claim 1 , serine claim 1 , threonine claim 1 , or valine at a position corresponding to position 246 of SEQ ID NO: 136.5. The non-naturally occurring polynucleotide encoding the non-naturally occurring polypeptide of claim 1 , wherein said non-naturally occurring polypeptide further comprises one or more amino acid differences relative to SEQ ID NO: 136 claim 1 , wherein said polypeptide further comprises one or more substitutions corresponding to substitutions in SEQ ID NO: ...

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Номер записи: 90
07-01-2021 дата публикации

A NOVEL PROMOTER AND A METHOD FOR PRODUCING L-AMINO ACID USING THE SAME

Номер: US20210002654A1
Автор: CHANG Jin Sook, CHOI Sun Hyoung, CHOI Yunjung, Kim Hyung Joon, Lee Ji Yeon, YOON Byoung Hoon
Принадлежит:

The present disclosure relates to a novel promoter and a method for producing L-amino acids using the promoter, and more specifically, to a novel polynucleotide having promoter activity, a vector and a microorganism of the genus comprising the polynucleotide, a method for producing L-amino acids using the microorganism, and a fermented composition. 1. A polynucleotide having promoter activity , wherein the 37nucleotide of the nucleotide sequence of SEQ ID NO: 2 is substituted with G.2. The polynucleotide according to claim 1 , wherein the polynucleotide consists of the nucleotide sequence of SEQ ID NO: 1.3. The polynucleotide according to claim 1 , wherein the polynucleotide is operably linked to a gene encoding a target protein.4. A vector comprising the polynucleotide of ; and a gene encoding a target protein operably linked to the polynucleotide.5. The vector of claim 4 , wherein the target protein is lactate dehydrogenase.6Corynebacterium. A microorganism of the genus claim 1 , comprising the polynucleotide of ; and a gene encoding a target protein operably linked to the polynucleotide.7. The microorganism according to claim 6 , wherein the polynucleotide consists of the nucleotide sequence of SEQ ID NO: 1.8. The microorganism according to claim 6 , wherein the target protein is lactate dehydrogenase.9CorynebacteriumCorynebacterium glutamicum.. The microorganism according to claims 6 , wherein the microorganism of the genus is10. A method for producing a target substance claims 6 , comprising:{'i': 'Corynebacterium', 'claim-ref': {'@idref': 'CLM-00006', 'claim 6'}, 'culturing the microorganism of the genus of in a medium; and'}recovering the target substance from the cultured medium.11. The method according to claim 8 , wherein the target substance is an amino acid.12Corynebacterium. A method for preparing a fermented composition claim 6 , comprising fermenting by culturing the microorganism of the genus of in a medium.13. A fermented composition prepared by the ...

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Номер записи: 91
07-01-2021 дата публикации

MODIFIED HOMOSERINE DEHYDROGENASE AND METHOD FOR PRODUCING HOMOSERINE OR L-AMINO ACID DERIVED FROM HOMOSERINE USING THE SAME

Номер: US20210002682A1
Автор: Huh Lan, KIM Hyo Jin, Kim Hyoung Joon, Kim Hyun Ah, LEE Ji Sun, LEE Seung Bin, Lim Sang Jo, Seo Chang Il
Принадлежит:

The present disclosure relates to modified homoserine dehydrogenase and a method for producing a homoserine-derived L-amino acid using the same. 1. A modified homoserine dehydrogenase , wherein in the amino acid sequence of SEQ ID NO: 1 , the amino acid at position 285 is substituted with isoleucine; the amino acid at position 398 is substituted with glutamine; or the amino acids at both positions are substituted with isoleucine and glutamine , respectively.2. The modified homoserine dehydrogenase according to claim 1 , wherein in the amino acid sequence of SEQ ID NO: 1 claim 1 , the amino acid at position 378 is further substituted with tryptophan.3. A polynucleotide encoding the modified homoserine dehydrogenase of .4Corynebacterium,. A microorganism of the genus comprising the modified homoserine dehydrogenase of .5CorynebacteriumCorynebacterium. The microorganism according to claim 4 , wherein the microorganism of the genus is a microorganism of the genus producing homoserine or a homoserine-derived L-amino acid.6. The microorganism according to claim 5 , wherein the homoserine-derived L-amino acid is at least one kind selected from the group consisting of L-threonine claim 5 , L-isoleucine claim 5 , O-acetyl homoserine claim 5 , and L-methionine.7Corynebacterium. The microorganism according to claim 4 , wherein the microorganism of the genus produces L-alanine.8CorynebacteriumCorynebacterium glutamicum.. The microorganism according to claim 4 , wherein the microorganism of the genus is9. A method for producing homoserine or a homoserine-derived L-amino acid claim 4 , comprising:{'claim-ref': {'@idref': 'CLM-00004', 'claim 4'}, 'culturing a microorganism of in a medium; and'}recovering homoserine or a homoserine-derived L-amino acid from the microorganism or medium.10. The method according to claim 9 , wherein the homoserine-derived L-amino acid is at least one kind selected from the group consisting of L-threonine claim 9 , L-isoleucine claim 9 , O-acetyl ...

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Номер записи: 92
03-01-2019 дата публикации

NOVEL P450-BM3 VARIANTS WITH IMPROVED ACTIVITY

Номер: US20190002847A1
Автор: Htwe Khin Yu Naing, Milczek Erika M., Mitchell Vesna, MOORE Jeffrey C., Osborne Robert, Zhang Xiyun
Принадлежит:

The present invention provides improved P450-BM3 variants with improved activity. In some embodiments, the P450-BM3 variants exhibit improved activity over a wide range of substrates. 1. A recombinant cytochrome P450-BM3 variant comprising a polypeptide sequence having at least 90% sequence identity to the polypeptide sequence set forth in SEQ ID NO: 44.2. The recombinant cytochrome P450-BM3 variant of claim 1 , wherein said variant oxidizes at least three organic substrates.3. The recombinant cytochrome P450-BM3 variant of claim 2 , wherein said organic substrate is selected from nifedipine claim 2 , propranolol claim 2 , verapamil claim 2 , and diclofenac.4. An isolated polynucleotide sequence encoding the recombinant cytochrome P450-BM3 variant of .5. The isolated polynucleotide sequence of claim 4 , wherein said sequence comprises the polynucleotide sequence of SEQ ID NO: 43.6. An expression vector comprising the polynucleotide sequence of .7. The vector of claim 6 , wherein said polynucleotide sequence is operably linked with regulatory sequences suitable for expression of said polynucleotide sequence in a suitable host cell.8. The vector of claim 6 , wherein said host cell is a prokaryotic or eukaryotic cell.9. The vector of claim 8 , wherein said host cell is a prokaryotic cell.10E. coli.. The vector of claim 8 , wherein said host cell is11. A host cell comprising the vector of .12. A method for producing at least one recombinant cytochrome P450-BM3 variant comprising culturing the host cell of under conditions such that a recombinant cytochrome P450-BM3 variant is produced.13. The method of claim 12 , further comprising the step of recovering said at least one recombinant cytochrome P450 variant. This application is a continuation of U.S. patent application Ser. No. 15/619,176, filed Jun. 9, 2017, which is a Divisional of U.S. patent application Ser. No. 14/794,249, filed Jul. 8, 2015, now U.S. Pat. No. 9,708,587, which claims the benefit of U.S. Provisional ...

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Номер записи: 93
01-01-2015 дата публикации

METHOD FOR PREPARING CYSTEINE OR A DERIVATIVE THEREOF USING A NOVEL O-PHOSPHOSERINE SULFHYDRYLASE

Номер: US20150004657A1
Автор: CHANG Jin Sook, JO Jae Hyun, KIM Hye Won, SONG Byeong Cheol
Принадлежит:

The present invention relates to a method for producing cysteine or derivatives thereof using novel O-phosphoserine sulfhydrylase. According to the present invention, a method for producing cysteine by novel O-phosphoserine sulfhydrylase (OPSS) using O-phosphoserine as a substrate is provided, and this method is advantageous in that cysteine can be simply and environmental-friendly produced in a high yield. 1. A method for producing cysteine or derivatives thereof , comprising the step of reacting O-phosphoserine (OPS) with a sulfide in the presence of O-phosphoserine sulfhydrylase (OPSS) having an amino acid sequence represented by SEQ ID NO. 1 or 2 , or a microorganism expressing the same , thereby producing cysteine or the derivatives thereof.2. The method according to claim 1 , wherein the OPSS is encoded by a polynucleotide having a nucleotide sequence selected from the group consisting of SEQ ID NOs. 9 to 12.3. The method according to claim 1 , wherein the OPS is purified OPS or a fermentation broth of a microorganism including OPS.4. The method according to claim 1 , wherein the sulfide is selected from the group consisting of NaS claim 1 , HS claim 1 , NaSH claim 1 , (NH)S and SO.5. The method according to claim 1 , wherein the sulfide is added at a molar concentration which is 0.1 to 3 times as high as that of OPS added in the reaction.6. The method according to claim 1 , wherein a cofactor during the reaction is further added as 0.001 to 2 mM pyridoxal-5′-phosphate (PLP) or 0.001 to 100 mM dithiothreitol (DTT).7. The method according to claim 1 , further comprising the step of separating and purifying the cysteine or derivatives thereof. The present invention relates to a method for producing cysteine or derivatives thereof using novel O-phosphoserine sulfhydrylase.Cysteine is an important amino acid in sulfur metabolism of all living organisms. It is used in the biosynthesis of proteins, such as hair keratin, glutathione, biotin, methionine and other ...

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Номер записи: 94
01-01-2015 дата публикации

SULFUR AMINO ACID-CONTAINING COMPOSITION

Номер: US20150004658A1
Автор: HARATA Masataka, Inagawa Yuto
Принадлежит: NISSHIN PHARMA INC.

Provision of a composition stably comprising a high concentration of sulfur amino acid derived from a plant belonging to the genus . A method for producing a sulfur amino acid-comprising composition comprising: heating a plant belonging to the genus ; treating the plant belonging to the genus thus heated with a γ-glutamyl bond cleaving enzyme; and subjecting the resulting enzyme-treated product to ion exchange chromatography. 1. A method for producing a sulfur amino acid-comprising composition comprising:{'i': 'Allium,', 'heating a plant belonging to the genus'}treating the heated plant with a γ-glutamyl bond cleaving enzyme to produce an enzyme-treated product, andsubjecting the enzyme-treated product to ion exchange chromatography.2. The method according to claim 1 , wherein the γ-glutamyl bond cleaving enzyme is γ-glutaminase claim 1 , γ-glutamyl transferase claim 1 , γ-glutamyl transpeptidase or γ-glutamyl peptidase.3. The method according to claim 1 , wherein a strongly acidic cation-exchange resin is used in the ion exchange chromatography.4. The method according claim 1 , wherein the sulfur amino acid is at least one selected from the group consisting of S-1-propenyl-L-cysteine sulfoxide claim 1 , S-propyl-L-cysteine sulfoxide claim 1 , S-methyl-L-cysteine sulfoxide and S-allyl-L-cysteine sulfoxide.5. The method according to claim 2 , wherein a strongly acidic cation-exchange resin is used in the ion exchange chromatography.6. The method according to claim 2 , wherein the sulfur amino acid is at least one selected from the group consisting of S-1-propenyl-L-cysteine sulfoxide claim 2 , S-propyl-L-cysteine sulfoxide claim 2 , S-methyl-L-cysteine sulfoxide and S-allyl-L-cysteine sulfoxide.7. The method according to claim 3 , wherein the sulfur amino acid is at least one selected from the group consisting of S-1-propenyl-L-cysteine sulfoxide claim 3 , S-propyl-L-cysteine sulfoxide claim 3 , S-methyl-L-cysteine sulfoxide and S-allyl-L-cysteine sulfoxide.8. The ...

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Номер записи: 95
20-01-2022 дата публикации

RECOMBINANT MICROORGANISM CAPABLE OF GROWING USING ONLY CARBON DIOXIDE AND FORMIC ACID AND METHOD FOR PRODUCING USEFUL SUBSTANCES USING THE RECOMBINANT MICROORGANISM

Номер: US20220017879A1
Автор: Ahn Jung Ho, BANG Junho, HWANG Chang Hun, LEE Jong An, LEE Sang Yup
Принадлежит:

Disclosed is a recombinant microorganism capable of growing using only carbon dioxide and formic acid by introducing and improving a metabolic pathway for synthesizing pyruvic acid from carbon dioxide and formic acid to enhance pyruvic acid synthesis efficiency and performing additional genetic manipulation, and a method for producing useful substances using the same. Advantageously, the recombinant microorganism is capable of synthesizing pyruvic acid, a C3 organic compound, at a remarkably improved rate, and in particular, grows well even in a medium containing only carbon dioxide and formic acid as carbon sources without a glucose supply, and is thereby capable of synthesizing pyruvic acid and various high value-added compounds using the same as an intermediate product in an economically efficient manner. 1. A recombinant microorganism , in which a gene encoding a glycine cleavage system transcriptional repressor , pyruvate formate lyase , or phosphoglycerate dehydrogenase is attenuated or deleted from a host microorganism having a formic acid assimilation pathway ,a gene encoding an enzyme involved in a glycine cleavage system reaction is enhancely expressed in the host microorganism having the formic acid assimilation pathway, anda gene encoding formate-tetrahydrofolate ligase, methenyl tetrahydrofolate cyclohydrolase, or methylene-tetrahydrofolate dehydrogenase is introduced into the host microorganism having the formic acid assimilation pathway.2Escherichia, Mannheimia, RhodobacterMethylobacterium. The recombinant microorganism according to claim 1 , wherein the host microorganism is selected from the group consisting of and genera.3. The recombinant microorganism according to claim 1 , wherein the expression of the gene encoding the enzyme involved in the glycine cleavage system reaction is enhanced by substituting a native promoter with a strong promoter.4. The recombinant microorganism according to claim 3 , wherein the strong promoter is selected from the ...

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Номер записи: 96
12-01-2017 дата публикации

METABOLIC TRANSISTOR IN BACTERIA

Номер: US20170009241A1
Автор: Bennett George N., San Ka-Yiu, Wu Hui
Принадлежит:

The disclosure relates to a metabolic transistor in microbes such as bacteria and yeast where a competitive pathway is introduced to compete with a product pathway for available carbon so as to control the carbon flux in the microbe. 1) A method of increasing the production of a product in a microbe , said method comprising:a) providing a microbe having a product pathway producing a product, wherein a competitive pathway competes with said product pathway for available carbon, said competitive pathway requiring a cofactor that is not rate limiting and not used in said product pathway;b) adding one or more diverting gene(s) under the control of a promoter to said microbe to directly or indirectly divert said cofactor away from said competitive pathway; and,c) allowing expression of said diverting gene(s) and reducing levels of said cofactor, and thus reducing levels of said competitive pathway;d) thereby increasing said product pathway and said product.4) The method of claim 1 , wherein said promoter is a constitutive promoter.5) The method of claim 1 , wherein said promoter is an inducible promoter.6) A method of controlling aerobic respiration in a microbe in the presence of O claim 1 , said method comprising:a) adding a diverting gene(s) to a microbe to divert substrates away from ubiquinone or thiamine or heme production, wherein said diverting gene(s) is under the control of a promoter; and,{'sub': '2', 'b) inducing said promoter, thereby allowing expression of said diverting gene(s), thus reducing ubiquinone levels and reducing aerobic respiration in the presence of 0.'}7) The method of claim 6 , wherein said diverting gene(s) includes the lycopene synthesis pathway.8) The method of claim 6 , wherein said diverting gene(s) include crtE claim 6 , crtB and crtI.9) The method of claim 6 , wherein said diverting gene encodes geranyl diphosphate:4-hydroxybenzoate geranyltransferase.10) The method of claim 6 , wherein said diverting gene is lePGT-1.11) The method of ...

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Номер записи: 97
08-01-2015 дата публикации

Modified Leucine Dehydrogenase

Номер: US20150010936A1
Автор: Toshimi Mizukoshi, Uno Tagami, Wataru HOSHINO, Yuya Kodama
Принадлежит: Ajinomoto Co Inc

The present invention provides a means and method useful for measurement of a total branched-chain amino acid concentration. Specifically, the present invention provides a modified enzyme in which at least one amino acid residue is mutated so as to improve a property of a leucine dehydrogenase which is associated with the measurement of the total branched-chain amino acids, such as, for example, substrate specificities of leucine dehydrogenase for total branched-chain amino acids, activity of leucine dehydrogenase for any branched-chain amino acids, and thermal stability of leucine dehydrogenase; and a method of analyzing the total branched-chain amino acids, comprising measuring the total branched-chain amino acids contained in a test sample using the modified enzyme.

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Номер записи: 98
08-01-2015 дата публикации

Method for Producing Basic Substance

Номер: US20150010962A1
Автор: Sugimoto Shinichi, Takeshita Ryo
Принадлежит: AJINOMOTO CO., INC.

A method for producing a basic substance by fermentation comprising culturing a microorganism having an ability to produce the basic substance in a liquid medium contained in a fermentation tank to produce and accumulate the basic substance in the medium, wherein amount of sulfate and/or chloride ions used as counter ions of the basic substance is reduced by adjusting total ammonia concentration in the medium to be within a specific concentration range during at least a part of the total period of culture process. 1. A method for producing a basic amino acid by fermentation comprising culturing a microorganism having an ability to produce the basic amino acid in a liquid medium contained in a fermentation tank to produce and accumulate the basic amino acid in the medium;wherein the amount of sulfate and/or chloride ions used as counter ions of the basic amino acid is reduced by adjusting the total ammonia concentration in the medium to be within a specific concentration range during at least a part of the total period of the culture process including a period where the pH of the medium increases due to shortage of the counter ions caused by accumulation of the objective basic amino acid;wherein the total ammonia concentration in the medium is adjusted so to ensure growth of the microorganism or the production of the basic amino acid, and at said concentration does not inhibit the production of the basic amino acid by the microorganism; and{'i': 'Escherichia coli', 'wherein the microorganism is an bacterium or a coryneform bacterium.'}2. The method according to claim 1 , wherein the total ammonia concentration in the medium is adjusted by adding ammonia or urea to the medium when the activity of the microorganism is reduced or ceases as determined based on the indicators: dissolved oxygen concentration in the medium claim 1 , consumption rate of carbon source in the medium claim 1 , turbidity of the medium claim 1 , productivity of the basic amino acid claim 1 , and ...

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Номер записи: 99
08-01-2015 дата публикации

Method for Producing Basic Substance

Номер: US20150010963A1
Автор: Sugimoto Shinichi, Takeshita Ryo
Принадлежит: AJINOMOTO CO., INC.

A method for producing a basic substance by fermentation comprising culturing a microorganism having an ability to produce the basic substance in a liquid medium contained in a fermentation tank to produce and accumulate the basic substance in the medium, wherein amount of sulfate and/or chloride ions used as counter ions of the basic substance is reduced by adjusting total ammonia concentration in the medium to be within a specific concentration range during at least a part of the total period of culture process. 1. A method for producing a basic amino acid by fermentation comprising culturing a microorganism having an ability to produce the basic amino acid in a liquid medium contained in a fermentation tank to produce and accumulate the basic amino acid in the medium;wherein the amount of sulfate and/or chloride ions used as counter ions of the basic amino acid is reduced by adjusting the total ammonia concentration in the medium to be within a specific concentration range during at least a part of the total period of the culture process including a period where the pH of the medium increases due to shortage of the counter ions caused by accumulation of the objective basic amino acid;wherein the total ammonia concentration in the medium is adjusted to be 300 mM or lower; andwherein the microorganism is a coryneform bacterium.2. The method according to claim 1 , wherein the coryneform bacterium has been modified so that the expression of lysE gene is increased.3. The method according to claim 2 , wherein the lysE gene is a DNA selected from the group consisting of:(i) a DNA encoding a protein comprising the amino acid sequence of SEQ ID NO: 10; and(ii) a DNA encoding a protein having a homology of 95% or more to the amino acid sequence of SEQ ID NO: 10.4. The method according to claim 1 , wherein the total ammonia concentration in the medium is adjusted by adding ammonia or urea to the medium when the activity of the microorganism is reduced or ceases as ...

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Номер записи: 100