CN104593394A - 具有α淀粉酶活性的酶及其使用方法 - Google Patents
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Classifications
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- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/14—Hydrolases (3)
- C12N9/24—Hydrolases (3) acting on glycosyl compounds (3.2)
- C12N9/2402—Hydrolases (3) acting on glycosyl compounds (3.2) hydrolysing O- and S- glycosyl compounds (3.2.1)
- C12N9/2405—Glucanases
- C12N9/2408—Glucanases acting on alpha -1,4-glucosidic bonds
- C12N9/2411—Amylases
- C12N9/2414—Alpha-amylase (3.2.1.1.)
- C12N9/2417—Alpha-amylase (3.2.1.1.) from microbiological source
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- A—HUMAN NECESSITIES
- A21—BAKING; EDIBLE DOUGHS
- A21D—TREATMENT OF FLOUR OR DOUGH FOR BAKING, e.g. BY ADDITION OF MATERIALS; BAKING; BAKERY PRODUCTS
- A21D8/00—Methods for preparing or baking dough
- A21D8/02—Methods for preparing dough; Treating dough prior to baking
- A21D8/04—Methods for preparing dough; Treating dough prior to baking treating dough with microorganisms or enzymes
- A21D8/042—Methods for preparing dough; Treating dough prior to baking treating dough with microorganisms or enzymes with enzymes
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/14—Hydrolases (3)
- C12N9/24—Hydrolases (3) acting on glycosyl compounds (3.2)
- C12N9/2402—Hydrolases (3) acting on glycosyl compounds (3.2) hydrolysing O- and S- glycosyl compounds (3.2.1)
- C12N9/2405—Glucanases
- C12N9/2408—Glucanases acting on alpha -1,4-glucosidic bonds
- C12N9/2411—Amylases
- C12N9/2414—Alpha-amylase (3.2.1.1.)
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
- C12P19/00—Preparation of compounds containing saccharide radicals
- C12P19/04—Polysaccharides, i.e. compounds containing more than five saccharide radicals attached to each other by glycosidic bonds
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
- C12P19/00—Preparation of compounds containing saccharide radicals
- C12P19/14—Preparation of compounds containing saccharide radicals produced by the action of a carbohydrase (EC 3.2.x), e.g. by alpha-amylase, e.g. by cellulase, hemicellulase
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Y—ENZYMES
- C12Y302/00—Hydrolases acting on glycosyl compounds, i.e. glycosylases (3.2)
- C12Y302/01—Glycosidases, i.e. enzymes hydrolysing O- and S-glycosyl compounds (3.2.1)
- C12Y302/01001—Alpha-amylase (3.2.1.1)
-
- Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y02—TECHNOLOGIES OR APPLICATIONS FOR MITIGATION OR ADAPTATION AGAINST CLIMATE CHANGE
- Y02E—REDUCTION OF GREENHOUSE GAS [GHG] EMISSIONS, RELATED TO ENERGY GENERATION, TRANSMISSION OR DISTRIBUTION
- Y02E50/00—Technologies for the production of fuel of non-fossil origin
- Y02E50/10—Biofuels, e.g. bio-diesel
Landscapes
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- Engineering & Computer Science (AREA)
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- Wood Science & Technology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Genetics & Genomics (AREA)
- Biotechnology (AREA)
- Microbiology (AREA)
- Biochemistry (AREA)
- General Health & Medical Sciences (AREA)
- General Engineering & Computer Science (AREA)
- Biomedical Technology (AREA)
- Molecular Biology (AREA)
- Medicinal Chemistry (AREA)
- Chemical Kinetics & Catalysis (AREA)
- General Chemical & Material Sciences (AREA)
- Food Science & Technology (AREA)
- Enzymes And Modification Thereof (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Measuring Or Testing Involving Enzymes Or Micro-Organisms (AREA)
- Peptides Or Proteins (AREA)
- Cereal-Derived Products (AREA)
- Bakery Products And Manufacturing Methods Therefor (AREA)
- Fodder In General (AREA)
- Paper (AREA)
- Detergent Compositions (AREA)
- Alcoholic Beverages (AREA)
- Apparatus Associated With Microorganisms And Enzymes (AREA)
- Chemical Or Physical Treatment Of Fibers (AREA)
- Jellies, Jams, And Syrups (AREA)
- Coloring Foods And Improving Nutritive Qualities (AREA)
Applications Claiming Priority (6)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US27049501P | 2001-02-21 | 2001-02-21 | |
| US27049601P | 2001-02-21 | 2001-02-21 | |
| US60/270,495 | 2001-02-21 | ||
| US60/270,496 | 2001-02-21 | ||
| US29112201P | 2001-05-14 | 2001-05-14 | |
| US60/291,122 | 2001-05-14 |
Related Parent Applications (1)
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Cited By (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN112384616A (zh) * | 2018-05-29 | 2021-02-19 | 巴斯夫欧洲公司 | 淀粉酶 |
Families Citing this family (99)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US20040005673A1 (en) * | 2001-06-29 | 2004-01-08 | Kevin Jarrell | System for manipulating nucleic acids |
| DE60042730D1 (de) * | 1999-01-05 | 2009-09-24 | Univ Boston | Verbessertes klonierungsverfahren |
| WO2002008408A2 (en) * | 2000-07-21 | 2002-01-31 | Trustees Of Boston University | Modular vector systems |
| US7435562B2 (en) | 2000-07-21 | 2008-10-14 | Modular Genetics, Inc. | Modular vector systems |
| WO2002010356A2 (de) | 2000-07-28 | 2002-02-07 | Henkel Kommanditgesellschaft Auf Aktien | Neues amylolytisches enzym aus bacillus sp. a 7-7 (dsm 12368) sowie wasch- und reinigungsmittel mit diesem neuen amylolytischen enzym |
| US7659102B2 (en) | 2001-02-21 | 2010-02-09 | Verenium Corporation | Amylases, nucleic acids encoding them and methods for making and using them |
| US7560126B2 (en) | 2001-02-21 | 2009-07-14 | Verenium Corporation | Amylases, nucleic acids encoding them and methods for making and using them |
| CA2833423C (en) | 2001-02-21 | 2019-03-19 | Verenium Corporation | Enzymes having alpha amylase activity and methods of use thereof |
| DE10138753B4 (de) * | 2001-08-07 | 2017-07-20 | Henkel Ag & Co. Kgaa | Wasch- und Reinigungsmittel mit Hybrid-Alpha-Amylasen |
| KR20040029122A (ko) * | 2001-08-27 | 2004-04-03 | 신젠타 파티서페이션즈 아게 | 자가-프로세싱 식물 및 식물 부분 |
| WO2004042006A2 (en) | 2002-10-31 | 2004-05-21 | Diversa Corporation | Amylases, nucleic acids encoding them and methods for making and using them |
| ES2278210T3 (es) | 2002-12-17 | 2007-08-01 | Novozymes A/S | Alfa-amilasas termoestables. |
| AU2015218541A1 (en) * | 2003-03-06 | 2015-10-29 | Basf Enzymes Llc | Amylases, nucleic acids encoding them and methods for making and using them |
| PL3023498T3 (pl) * | 2003-03-06 | 2019-05-31 | Basf Enzymes Llc | Amylazy, kodujące je kwasy nukleinowe i sposoby ich wytwarzania i zastosowania |
| MXPA05009566A (es) * | 2003-03-06 | 2005-12-14 | Diversa Corp | Amilasas, acidos nucleicos que las codifican, y metodos para hacerlas y usarlas. |
| JP4728950B2 (ja) * | 2003-03-10 | 2011-07-20 | ジェネンコー・インターナショナル・インク | プレバイオティックであるイソマルトオリゴ糖を含む穀物組成物、及び、この製造方法、並びに、その用途 |
| DE602004026733D1 (de) * | 2003-06-13 | 2010-06-02 | Danisco | Pseudomonas-polypeptidvarianten mit einer nicht maltogenen exoamylaseaktivität und ihre verwendung bei der herstellung von lebensmittelprodukten |
| WO2005001064A2 (en) | 2003-06-25 | 2005-01-06 | Novozymes A/S | Polypeptides having alpha-amylase activity and polypeptides encoding same |
| US7618795B2 (en) | 2003-06-25 | 2009-11-17 | Novozymes A/S | Starch process |
| WO2004113551A1 (en) * | 2003-06-25 | 2004-12-29 | Novozymes A/S | Process for the hydrolysis of starch |
| US8143048B2 (en) | 2003-07-07 | 2012-03-27 | Danisco A/S | Exo-specific amylase polypeptides, nucleic acids encoding those polypeptides and uses thereof |
| ATE408674T1 (de) * | 2003-07-07 | 2008-10-15 | Danisco As Danisco Intellectua | Varianten der nicht maltogenen exoamylase aus pseudomonas umfassender lebensmittelzusatz |
| US7169257B2 (en) * | 2003-11-12 | 2007-01-30 | Kemira Chemicals, Inc. | Method of deinking waste paper using a reduced alkali system |
| CA2558603A1 (en) * | 2004-03-08 | 2005-10-20 | Syngenta Participations Ag | Self-processing plants and plant parts |
| US20050257932A1 (en) * | 2004-05-19 | 2005-11-24 | Davidson Eric A | Filter cake degradation compositions and associated methods |
| AU2011203198B2 (en) * | 2004-07-07 | 2013-01-10 | Dupont Nutrition Biosciences Aps | Polypeptide |
| JP2008505632A (ja) * | 2004-07-07 | 2008-02-28 | ダニスコ エイ/エス | 非マルトース生成エキソアミラーゼ改変体 |
| US20060084150A1 (en) * | 2004-09-29 | 2006-04-20 | Qunyu Gao | Method for manufacturing maltose-rich products |
| ATE540110T1 (de) * | 2004-11-11 | 2012-01-15 | Modular Genetics Inc | Oligonukleotid-leiterkonstruktion und system zur erzeugung von molekularer vielfalt |
| US20060147581A1 (en) | 2004-12-22 | 2006-07-06 | Novozymes A/S | Hybrid enzymes |
| JP2008523830A (ja) | 2004-12-22 | 2008-07-10 | ノボザイムス アクティーゼルスカブ | ハイブリッド酵素 |
| CA2599381C (en) * | 2005-03-16 | 2013-10-22 | Syngenta Participations Ag | Corn event 3272 and methods for detection thereof |
| US20070184472A1 (en) * | 2005-06-08 | 2007-08-09 | Toagosei Co., Ltd | Method of purifying environmental dna and method of efficiently screening for protein-encoding gene from environmental dna |
| US8030050B2 (en) | 2005-07-07 | 2011-10-04 | Danisco A/S | Modified amylases from Pseudomonas species |
| JP5448812B2 (ja) | 2006-06-19 | 2014-03-19 | デュポン ニュートリション バイオサイエンシーズ エーピーエス | ポリペプチド |
| US20080014616A1 (en) * | 2006-07-11 | 2008-01-17 | Kevin Jarrell | Methods of introducing targeted diversity into nucleic acid molecules |
| AU2007356171B8 (en) * | 2006-08-04 | 2014-01-16 | Bp Corporation North America Inc. | Glucanases, nucleic acids encoding them, and methods for making and using them |
| US7808342B2 (en) * | 2006-10-02 | 2010-10-05 | Skyworks Solutions, Inc. | Harmonic phase tuning filter for RF switches |
| ES2575912T3 (es) * | 2006-12-21 | 2016-07-04 | Basf Enzymes Llc | Amilasas y glucoamilasas, ácidos nucleicos que las codifican y métodos para formarlas y utilizarlas |
| WO2008150880A1 (en) * | 2007-06-01 | 2008-12-11 | Syngenta Participations Ag | Process for starch liquefaction and fermentation |
| US7727726B2 (en) * | 2007-06-01 | 2010-06-01 | Syngenta Participations Ag | Process for starch liquefaction and fermentation |
| US7915020B2 (en) * | 2007-06-01 | 2011-03-29 | Syngenta Participations Ag | Process for starch liquefaction and fermentation |
| EP2240577A2 (en) | 2008-01-02 | 2010-10-20 | Danisco US Inc. | A process of obtaining ethanol without glucoamylase using pseudomonas saccharophila g4-amylase and variants thereof |
| US9816119B2 (en) | 2008-02-29 | 2017-11-14 | Syngenta Participations Ag | Methods for starch hydrolysis |
| DK2297312T3 (da) * | 2008-06-06 | 2013-12-16 | Danisco Us Inc | Alpha-amylasevarianter af Bacillus subtilis og fremgangsmåder til anvendelse heraf |
| MX2010013122A (es) | 2008-06-06 | 2011-01-21 | Danisco Inc | Composicion de enzima de sacarificacion y metodo de sacarificacion de la misma. |
| MX2010013108A (es) | 2008-06-06 | 2010-12-21 | Danisco Inc | Produccion de glucosa a partir de almidon usando alfa-amilasas de bacillus subtilis. |
| US7666457B1 (en) | 2008-08-19 | 2010-02-23 | Delavau Llc | Dry mixes comprising glycerine |
| CN102341495A (zh) * | 2009-03-10 | 2012-02-01 | 丹尼斯科美国公司 | 巨大芽孢杆菌菌株DSM90相关的α-淀粉酶及其使用方法 |
| BRPI1013388A2 (pt) * | 2009-04-01 | 2019-04-09 | Danisco Us Inc | composição de limpeza que compreende uma alfa-amilase e uma protease e método de limpeza de um tecido ou superficie dura |
| MX2011011911A (es) * | 2009-05-19 | 2011-12-08 | Danisco | Polipeptidos de amilasa. |
| CA2771071C (en) * | 2009-08-07 | 2020-03-10 | Danisco Us Inc. | Alpha-amylase blend for starch processing and method of use thereof |
| CA2778471A1 (en) * | 2009-10-23 | 2011-04-28 | Danisco Us Inc. | Methods for reducing blue saccharide |
| WO2011072117A1 (en) | 2009-12-09 | 2011-06-16 | The Procter & Gamble Company | Fabric and home care products |
| EP2529012A2 (en) * | 2010-01-25 | 2012-12-05 | Syngenta Participations AG | Compositions and methods relating to dual activity enzymes having xylanase and cellulase activity |
| EP3543333B1 (en) * | 2011-06-30 | 2022-01-05 | Novozymes A/S | Method for screening alpha-amylases |
| US9672126B2 (en) | 2011-12-15 | 2017-06-06 | Sybase, Inc. | Hybrid data replication |
| US20130159253A1 (en) * | 2011-12-15 | 2013-06-20 | Sybase, Inc. | Directing a data replication environment through policy declaration |
| GB2499463B (en) | 2012-01-31 | 2014-04-02 | Verenium Corp | Reduced sugar syrups and methods of making reduced sugar syrups |
| DK4026902T3 (da) | 2012-06-08 | 2025-07-14 | Danisco Us Inc | Variante alfa-amylaser med øget aktivitet på stivelsespolymerer |
| BR112015023620B1 (pt) | 2013-03-15 | 2021-06-22 | Grain Processing Corporation | Preparação de malto-oligossacarídeos |
| US20160186102A1 (en) * | 2013-10-03 | 2016-06-30 | Danisco Us Inc. | Alpha-amylases from exiguobacterium, and methods of use, thereof |
| RU2762075C2 (ru) | 2015-04-10 | 2021-12-15 | Зингента Партисипейшнс Аг | Кормовые композиции для животных и способы их применения |
| EP3334862A2 (en) * | 2015-08-14 | 2018-06-20 | Basf Se | Aqueous surface treatment composition for paper and board |
| FR3045055B1 (fr) | 2015-12-10 | 2020-02-21 | Roquette Freres | Hydrolysat d'amidon de basse viscosite presentant un comportement a la retrogradation ameliore |
| BR112018011954A2 (pt) * | 2015-12-18 | 2018-12-04 | Basf Enzymes Llc | formulação líquida de enzima, método para produzir uma formulação líquida de enzima, e, uso de uma formulação líquida de enzima. |
| DE102016208466A1 (de) | 2016-05-18 | 2017-11-23 | Henkel Ag & Co. Kgaa | Verbesserte Waschleistung durch eine neue alpha-Amylase aus Rhizoctonia solani |
| DE102016209880A1 (de) | 2016-06-06 | 2017-12-07 | Henkel Ag & Co. Kgaa | Neue Amylasen |
| WO2017220787A1 (en) * | 2016-06-24 | 2017-12-28 | Evaxion Biotech Aps | Vaccines against aearomonas salmonicida infection |
| CN106011107B (zh) * | 2016-06-30 | 2019-09-10 | 安徽工程大学 | 一种耐碱性α-淀粉酶及其基因工程菌的构建方法和应用 |
| CA3036575A1 (en) | 2016-09-16 | 2018-03-22 | Basf Se | Methods of modifying pulp comprising cellulase enzymes and products thereof |
| DE102016221851A1 (de) | 2016-11-08 | 2018-05-09 | Henkel Ag & Co. Kgaa | Amylase für Wasch- und Reinigungsmittelanwendungen |
| CA3067218A1 (en) | 2017-06-16 | 2018-12-20 | Basf Enzymes Llc | Method for increasing oil yield during ethanol production |
| WO2019075028A1 (en) | 2017-10-12 | 2019-04-18 | Syngenta Participations Ag | ENHANCED ANIMAL FEEDING COMPOSITIONS AND METHODS OF USE |
| CN119955763A (zh) | 2017-10-25 | 2025-05-09 | 巴斯夫欧洲公司 | β-淀粉酶 |
| DE102017220757A1 (de) | 2017-11-21 | 2019-05-23 | Henkel Ag & Co. Kgaa | Amylase und eine solche enthaltendes Wasch- oder Reinigungsmittel |
| MX2020009504A (es) * | 2018-03-13 | 2021-01-15 | Lallemand Hungary Liquidity Man Llc | Levadura inactivada y producto de levadura para mejorar el rendimiento de fermentación. |
| MX2020009437A (es) * | 2018-03-13 | 2021-01-08 | Lallemand Hungary Liquidity Man Llc | Alfa-amilasas termoestables expresadas por levadura para hidrólisis de almidón. |
| BR112020021692A2 (pt) | 2018-04-26 | 2021-01-26 | Basf Se | polipeptídeo tendo atividade de lipase, polipeptídeo híbrido, composição, polinucleotídeo variante, método para fabricar a variante de polipeptídeo, e, uso do polipeptídeo |
| US20210115422A1 (en) * | 2018-05-03 | 2021-04-22 | Basf Se | Amylase enzymes |
| US11530427B2 (en) * | 2018-05-25 | 2022-12-20 | Basf Se | Uses of surfactants in starch processing |
| DE102018208446A1 (de) | 2018-05-29 | 2019-12-05 | Henkel Ag & Co. Kgaa | Verbesserte Waschleistung durch eine neue alpha-Amylase aus Fomes fomentarius (Ffo) |
| DE102018208444A1 (de) | 2018-05-29 | 2019-12-05 | Henkel Ag & Co. Kgaa | Verbesserte Waschleistung durch eine neue alpha-Amylase aus Trametes hirsuta (Thi) |
| DE102018208445A1 (de) | 2018-05-29 | 2019-12-05 | Henkel Ag & Co. Kgaa | Verbesserte Waschleistung durch eine neue alpha-Amylase aus Fomitopsis pinicola (Fpi) |
| DE102018208443A1 (de) | 2018-05-29 | 2019-12-05 | Henkel Ag & Co. Kgaa | Verbesserte Waschleistung durch eine neue alpha-Amylase Irpex lacteus (IIa) |
| US20220186234A1 (en) | 2019-02-20 | 2022-06-16 | Basf Se | Industrial Fermentation Process for Bacillus Using Defined Medium and Trace Element Feed |
| EP3927837A1 (en) | 2019-02-20 | 2021-12-29 | Basf Se | Industrial fermentation process for bacillus using defined medium and magnesium feed |
| US20220186200A1 (en) | 2019-03-11 | 2022-06-16 | Basf Se | Amylases and methods for making and using them |
| US20220162576A1 (en) | 2019-03-25 | 2022-05-26 | Basf Se | Amylase enzymes |
| US20220170001A1 (en) | 2019-03-25 | 2022-06-02 | Basf Se | Amylase Enzymes |
| WO2020193532A1 (en) | 2019-03-25 | 2020-10-01 | Basf Se | Cleaning composition having amylase enzymes |
| WO2020219450A1 (en) | 2019-04-23 | 2020-10-29 | Basf Se | Beta-amylase variants |
| US11352854B2 (en) | 2019-05-13 | 2022-06-07 | Halliburton Energy Services, Inc. | Injectivity and production improvement in oil and gas fields |
| WO2020247834A1 (en) * | 2019-06-05 | 2020-12-10 | Danisco Us Inc | Methods for improving the amino acid content of animal feed products |
| DK3983425T3 (da) | 2019-06-13 | 2025-12-15 | Basf Se | Fremgangsmåde til udvinding af et protein fra en fermenteringsbouillon ved hjælp af en divalent kation |
| MX2022000253A (es) | 2019-07-05 | 2022-02-03 | Basf Se | Proceso de fermentacion industrial para celulas microbianas mediante el uso de un precultivo de alimentacion por lotes. |
| WO2021032881A1 (en) | 2019-08-22 | 2021-02-25 | Basf Se | Amylase variants |
| US20250311734A1 (en) | 2022-05-14 | 2025-10-09 | Novozymes A/S | Compositions and Methods for Preventing, Treating, Suppressing and/or Eliminatting Phytopathogenic Infestations and Infections |
| CN119060988B (zh) * | 2024-09-30 | 2025-08-22 | 南京大学 | 一种耐盐的α-淀粉酶突变体及其应用 |
Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN1222938A (zh) * | 1996-05-14 | 1999-07-14 | 金克克国际有限公司 | 经修饰具有改变了的钙离子吉合性质的α-淀粉酶 |
| CN1233286A (zh) * | 1996-10-11 | 1999-10-27 | 诺沃挪第克公司 | a-淀粉酶与纤维素结合结构域融合以用于淀粉降解 |
Family Cites Families (48)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US3847740A (en) * | 1972-10-02 | 1974-11-12 | Cpc International Inc | Process for the production of levulose-bearing syrups |
| JPS5823799A (ja) | 1981-08-03 | 1983-02-12 | 株式会社林原生物化学研究所 | 高純度マルト−スの製造方法 |
| JPS5872598A (ja) * | 1981-10-26 | 1983-04-30 | Hayashibara Biochem Lab Inc | 高純度イソマルト−スの製造方法 |
| US4557927A (en) * | 1983-03-10 | 1985-12-10 | Kabushiki Kaisha Hoyashibara | Food products and process for producing same |
| DE3688920T4 (de) | 1985-07-03 | 1995-08-31 | Genencor Int | Hybride Polypeptide und Verfahren zu deren Herstellung. |
| JPS62104580A (ja) | 1985-10-30 | 1987-05-15 | Kunio Yamane | 高耐熱性酵素発現dna |
| FI93859C (fi) * | 1985-12-03 | 1995-06-12 | Gist Brocades Nv | Menetelmä glukoosisiirappien ja puhdistettujen tärkkelysten tuottamiseksi vehnän ja muiden viljakasvien pentosaaneja sisältävistä tärkkelyksistä |
| GB8609288D0 (en) * | 1986-04-16 | 1986-05-21 | Ici Plc | Debranching enzyme |
| DK311186D0 (da) | 1986-06-30 | 1986-06-30 | Novo Industri As | Enzymer |
| US4946778A (en) | 1987-09-21 | 1990-08-07 | Genex Corporation | Single polypeptide chain binding molecules |
| JP2696537B2 (ja) | 1988-10-28 | 1998-01-14 | 東和化成工業株式会社 | 高純度マルトースの製造方法 |
| EP0528881A4 (en) | 1990-04-24 | 1993-05-26 | Stratagene | Methods for phenotype creation from multiple gene populations |
| US6582908B2 (en) * | 1990-12-06 | 2003-06-24 | Affymetrix, Inc. | Oligonucleotides |
| EP0599859A1 (en) | 1991-06-25 | 1994-06-08 | Novo Nordisk A/S | Mammalian pancreatic lipase and variant thereof |
| EP0691344B1 (en) | 1992-12-28 | 2003-03-19 | Kabushiki Kaisha Hayashibara Seibutsu Kagaku Kenkyujo | Purification of trehalose |
| PT867504E (pt) | 1993-02-11 | 2003-08-29 | Genencor Int | Alfa-amilase estavel a oxidacao |
| JP3559585B2 (ja) | 1993-06-03 | 2004-09-02 | 株式会社林原生物化学研究所 | トレハロース遊離酵素とその製造方法並びに用途 |
| EP0648843A1 (en) | 1993-10-01 | 1995-04-19 | Takara Shuzo Co. Ltd. | DNA encoding a hyperthermostable alpha-amylase |
| JPH07143880A (ja) * | 1993-10-01 | 1995-06-06 | Takara Shuzo Co Ltd | 超耐熱性α−アミラーゼ遺伝子 |
| CN1189558C (zh) * | 1993-10-08 | 2005-02-16 | 诺沃奇梅兹有限公司 | 淀粉酶变体 |
| DE69626976T2 (de) | 1995-06-02 | 2004-03-04 | Novozymes A/S | BEHANDLUNG EINER PROTEINLÖSUNG MIT A1/Fe UND ANSCHLIESENDE MEMBRANKONZENTRATION |
| US5736499A (en) | 1995-06-06 | 1998-04-07 | Genencor International, Inc. | Mutant A-amylase |
| JPH09173077A (ja) * | 1995-07-20 | 1997-07-08 | Tadayuki Imanaka | 超耐熱性酸性α−アミラーゼおよび該α−アミラーゼ産生遺伝子を含むDNA断片 |
| US5939250A (en) | 1995-12-07 | 1999-08-17 | Diversa Corporation | Production of enzymes having desired activities by mutagenesis |
| US5965408A (en) | 1996-07-09 | 1999-10-12 | Diversa Corporation | Method of DNA reassembly by interrupting synthesis |
| US6479258B1 (en) * | 1995-12-07 | 2002-11-12 | Diversa Corporation | Non-stochastic generation of genetic vaccines |
| US5789228A (en) * | 1996-05-22 | 1998-08-04 | Diversa Corporation | Endoglucanases |
| AU7107798A (en) * | 1997-04-09 | 1998-10-30 | Michigan State University | Hyperthermostable alpha-amylase |
| CN1163597C (zh) * | 1997-10-30 | 2004-08-25 | 诺维信公司 | α-淀粉酶突变体 |
| AUPP209298A0 (en) * | 1998-03-02 | 1998-03-26 | Uniphase Fibre Components Pty Limited | Grating writing techniques |
| FR2778412B1 (fr) | 1998-05-05 | 2002-08-09 | Univ Reims Champagne Ardennes | Procede pour preparer une enzyme alpha-amylase thermophile et enzyme ainsi obtenue |
| EP1090136B1 (en) | 1998-06-24 | 2006-05-31 | Sanofi-Aventis Deutschland GmbH | Mumbaistatin, a process for its production and its use as a pharmaceutical |
| WO1999067406A1 (en) | 1998-06-25 | 1999-12-29 | Applied Phytologics, Inc. | Plant selectable marker and plant transformation method |
| WO2000058508A2 (en) | 1999-03-25 | 2000-10-05 | Genset | Biallelic markers related to genes involved in drug metabolism |
| DK1818396T3 (da) * | 1999-03-30 | 2014-08-11 | Novozymes As | Alpha-amylase varianter |
| KR20030007669A (ko) * | 2000-05-22 | 2003-01-23 | 가부시끼가이샤 하야시바라 세이부쓰 가가꾸 겐꾸조 | α-이소말토실 전이 효소와 그 제조 방법 및 용도 |
| WO2002029079A2 (en) | 2000-10-04 | 2002-04-11 | Maxygen, Inc. | Enantioselective production of amino carboxylic acids |
| CA2833423C (en) * | 2001-02-21 | 2019-03-19 | Verenium Corporation | Enzymes having alpha amylase activity and methods of use thereof |
| US7560126B2 (en) * | 2001-02-21 | 2009-07-14 | Verenium Corporation | Amylases, nucleic acids encoding them and methods for making and using them |
| US7659102B2 (en) * | 2001-02-21 | 2010-02-09 | Verenium Corporation | Amylases, nucleic acids encoding them and methods for making and using them |
| DE10131441A1 (de) | 2001-06-29 | 2003-01-30 | Henkel Kgaa | Eine neue Gruppe von alpha-Amylasen sowie ein Verfahren zur Identifizierung und Gewinnung neuer alpha-Amylasen |
| AU2002319764A1 (en) | 2001-08-03 | 2003-02-17 | Elitra Pharmaceuticals, Inc. | Nucleic acids of aspergillus fumigatus encoding industrial enzymes and methods of use |
| KR20040029122A (ko) * | 2001-08-27 | 2004-04-03 | 신젠타 파티서페이션즈 아게 | 자가-프로세싱 식물 및 식물 부분 |
| US20040025917A1 (en) * | 2002-08-06 | 2004-02-12 | Jeremy Gin | Mobility-aid apparatus and method using tabs on non-boundary region |
| MXPA05009566A (es) | 2003-03-06 | 2005-12-14 | Diversa Corp | Amilasas, acidos nucleicos que las codifican, y metodos para hacerlas y usarlas. |
| MX2011006166A (es) | 2008-12-15 | 2011-10-10 | Danisco Inc | Alfa-amilasas hibridas. |
| WO2012155131A1 (en) | 2011-05-12 | 2012-11-15 | Sealy Technology, Llc | Advanced conformance encased coil spring units |
| CN109738224B (zh) | 2013-06-21 | 2021-07-16 | 伯乐生命医学产品有限公司 | 具有流体收集管的微流体系统 |
-
2002
- 2002-02-21 CA CA2833423A patent/CA2833423C/en not_active Expired - Lifetime
- 2002-02-21 WO PCT/US2002/005538 patent/WO2002068597A2/en not_active Ceased
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- 2002-02-21 CA CA3032990A patent/CA3032990C/en not_active Expired - Lifetime
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- 2002-02-21 US US10/081,872 patent/US7407677B2/en not_active Expired - Lifetime
- 2002-02-21 PT PT02706401T patent/PT1370674E/pt unknown
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- 2002-02-21 US US10/081,739 patent/US7273740B2/en not_active Expired - Lifetime
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- 2002-02-21 ES ES10184478.5T patent/ES2650636T3/es not_active Expired - Lifetime
- 2002-02-21 DK DK10184381.1T patent/DK2333097T3/da active
- 2002-02-21 CA CA2438884A patent/CA2438884C/en not_active Expired - Lifetime
- 2002-02-21 EP EP02723192.7A patent/EP1392815B1/en not_active Expired - Lifetime
- 2002-02-21 EP EP09171688.6A patent/EP2169076B1/en not_active Expired - Lifetime
- 2002-02-21 CN CN201410559804.5A patent/CN104593394A/zh active Pending
- 2002-02-21 JP JP2002568693A patent/JP2004533220A/ja not_active Withdrawn
- 2002-02-21 AU AU2002240489A patent/AU2002240489C1/en not_active Ceased
- 2002-02-21 EP EP02706401A patent/EP1370674B1/en not_active Expired - Lifetime
- 2002-02-21 CA CA2897239A patent/CA2897239A1/en not_active Abandoned
- 2002-02-21 ES ES10184415.7T patent/ES2604329T3/es not_active Expired - Lifetime
- 2002-02-21 DK DK09171688.6T patent/DK2169076T3/en active
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- 2002-02-21 CA CA3081363A patent/CA3081363A1/en not_active Abandoned
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Patent Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN1222938A (zh) * | 1996-05-14 | 1999-07-14 | 金克克国际有限公司 | 经修饰具有改变了的钙离子吉合性质的α-淀粉酶 |
| CN1233286A (zh) * | 1996-10-11 | 1999-10-27 | 诺沃挪第克公司 | a-淀粉酶与纤维素结合结构域融合以用于淀粉降解 |
Non-Patent Citations (3)
| Title |
|---|
| 登录号: ""GenBank Accession No:AF017454.1"", 《GENBANK》 * |
| 登录号: ""GenBank Accession No:AF068255.1"", 《GENBANK》 * |
| 登录号: ""GenBank Accession No:D83793.1"", 《GENBANK》 * |
Cited By (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN112384616A (zh) * | 2018-05-29 | 2021-02-19 | 巴斯夫欧洲公司 | 淀粉酶 |
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