CN101550410A - 葡糖淀粉酶变体 - Google Patents
葡糖淀粉酶变体 Download PDFInfo
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- CN101550410A CN101550410A CNA2009101412582A CN200910141258A CN101550410A CN 101550410 A CN101550410 A CN 101550410A CN A2009101412582 A CNA2009101412582 A CN A2009101412582A CN 200910141258 A CN200910141258 A CN 200910141258A CN 101550410 A CN101550410 A CN 101550410A
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- Prior art keywords
- glucoamylase
- ser
- thr
- ala
- variant
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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
- C12N9/2428—Glucan 1,4-alpha-glucosidase (3.2.1.3), i.e. glucoamylase
-
- 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
- C12P19/20—Preparation of compounds containing saccharide radicals produced by the action of an exo-1,4 alpha-glucosidase, e.g. dextrose
-
- 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
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- Chemical Kinetics & Catalysis (AREA)
- General Chemical & Material Sciences (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Enzymes And Modification Thereof (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
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| CNB008101329A Division CN100510067C (zh) | 1999-07-09 | 2000-07-07 | 葡糖淀粉酶变体 |
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| CNB008101329A Expired - Fee Related CN100510067C (zh) | 1999-07-09 | 2000-07-07 | 葡糖淀粉酶变体 |
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Families Citing this family (116)
| Publication number | Priority date | Publication date | Assignee | Title |
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| US6352851B1 (en) | 1998-07-15 | 2002-03-05 | Novozymes A/S | Glucoamylase variants |
| AR029759A1 (es) * | 1999-07-09 | 2003-07-16 | Novozymes As | Variante de glucoamilasa original, una construccion de adn, un vector de expresion recombinante, una celula, un proceso para convertir almidon, uso de una variante de glucoamilasa para un proceso de fermentacion y metodo para mejorar la estabilidad termica. |
| CA2702204C (en) | 2000-08-01 | 2011-09-06 | Novozymes A/S | Alpha-amylase mutants with altered properties |
| EP3000881A3 (en) | 2001-05-15 | 2016-07-20 | Novozymes A/S | Alpha-amylase variant with altered properties |
| WO2003029449A2 (en) * | 2001-10-01 | 2003-04-10 | Novozymes A/S | Glucoamylase variants |
| JP4897186B2 (ja) * | 2002-03-27 | 2012-03-14 | 花王株式会社 | 変異アルカリセルラーゼ |
| DE60310264T2 (de) | 2002-12-17 | 2007-07-05 | Novozymes A/S | Thermostabile alpha-amylase |
| US7579177B2 (en) | 2003-05-30 | 2009-08-25 | Novozymes A/S | Alcohol product processes |
| EP2292744A1 (en) | 2003-07-07 | 2011-03-09 | Genencor International, Inc. | Thermostable amylase polypeptides, nucleic acids encoding those polypeptides and uses thereof |
| US8143048B2 (en) | 2003-07-07 | 2012-03-27 | Danisco A/S | Exo-specific amylase polypeptides, nucleic acids encoding those polypeptides and uses thereof |
| MXPA06004463A (es) | 2003-10-28 | 2006-06-27 | Novozymes North America Inc | Enzimas hibridas. |
| DE102004026152A1 (de) * | 2004-05-28 | 2005-12-15 | Basf Ag | Fermentative Herstellung von Feinchemikalien |
| CN101068921A (zh) * | 2004-07-07 | 2007-11-07 | 丹尼斯科公司 | 多肽 |
| MX2007007107A (es) | 2004-12-22 | 2007-08-08 | Novozymes North America Inc | Polipeptidos que tienen actividad de glucoamilasa y polinucleotidos que los codifican. |
| US8030050B2 (en) | 2005-07-07 | 2011-10-04 | Danisco A/S | Modified amylases from Pseudomonas species |
| CN101268195A (zh) | 2005-09-20 | 2008-09-17 | 诺维信北美公司 | 产生发酵产物的方法 |
| WO2007076388A2 (en) | 2005-12-22 | 2007-07-05 | Novozymes North America, Inc. | Processes for producing a fermentation product |
| CN100443589C (zh) * | 2005-12-30 | 2008-12-17 | 湖南鸿鹰祥生物工程股份有限公司 | 高转化率高纯度糖化酶浓缩液的生产方法 |
| US8076112B2 (en) | 2006-03-22 | 2011-12-13 | Novozymes A/S | Fermentation processes |
| AU2007262442B2 (en) | 2006-06-19 | 2012-11-01 | Dupont Nutrition Biosciences Aps | Polypeptide |
| EP2061882A2 (en) | 2006-10-10 | 2009-05-27 | Danisco US, INC., Genencor Division | Glucoamylase variants with altered properties |
| EP3219804B1 (en) | 2007-04-24 | 2019-07-17 | Novozymes North America, Inc. | Detoxifying pre-treated lignocellulose-containing materials |
| CN101796247B (zh) | 2007-09-03 | 2014-01-22 | 诺维信公司 | 脱毒和再循环在含木素纤维素材料的预处理中使用的洗涤溶液 |
| US8592194B2 (en) | 2007-10-09 | 2013-11-26 | Danisco Us Inc. | Glucoamylase variants with altered properties |
| PL2481796T3 (pl) * | 2007-10-09 | 2014-11-28 | Danisco Us Inc | Odmiany glukoamylazy |
| BRPI0820483B1 (pt) * | 2007-11-20 | 2022-04-12 | Danisco Us Inc | Variantes de glicoamilase com propriedades alteradas e composição compreendendo as mesmas |
| WO2009129086A2 (en) * | 2008-04-18 | 2009-10-22 | New England Biolabs, Inc. | Endoglycosidases that cleave o-linked glycans |
| MX2010013113A (es) | 2008-06-06 | 2010-12-21 | Danisco Inc | Variantes de alfa-amilasa geobacillus stearothermophilus con propiedades mejoradas. |
| CA2726688A1 (en) | 2008-06-23 | 2010-01-21 | Novozymes A/S | Processes for producing fermentation products |
| US20110165617A1 (en) | 2008-09-30 | 2011-07-07 | Novozymes North America, Inc. | Enzymatic Hydrolysis Of Pretreated Lignocellulose-Containing Material With Distillers Dried Grains |
| WO2010059413A2 (en) | 2008-11-20 | 2010-05-27 | Novozymes, Inc. | Polypeptides having amylolytic enhancing activity and polynucleotides encoding same |
| EP2384365A2 (en) | 2008-12-30 | 2011-11-09 | Novozymes North America, Inc. | Improvement of enzymatic hydrolysis of pretreated lignocellulose-containing material with dissolved air flotation sludge |
| WO2010078392A2 (en) | 2008-12-31 | 2010-07-08 | Novozymes North America, Inc. | Processes of producing fermentation products |
| CA2766720A1 (en) | 2009-07-07 | 2011-01-13 | Novozymes A/S | Process for treating a substrate with an enzyme |
| CA2768315A1 (en) | 2009-07-17 | 2011-01-20 | Novozymes A/S | A method of analyzing cellulose decay in cellulosic material hydrolysis |
| AR077942A1 (es) * | 2009-08-19 | 2011-10-05 | Danisco | Variantes de glucoamilasa |
| WO2011039324A1 (en) | 2009-09-30 | 2011-04-07 | Novozymes A/S | Steamed bread preparation methods and steamed bread improving compositions |
| CN102933227A (zh) | 2009-12-22 | 2013-02-13 | 诺维信公司 | 包含增强性多肽和淀粉降解酶的组合物及其用途 |
| EP2529022A1 (en) | 2010-01-29 | 2012-12-05 | Novozymes A/S | Biogas production process with enzymatic pre-treatment |
| WO2011100161A1 (en) | 2010-02-09 | 2011-08-18 | Novozymes North America, Inc. | Addition of alpha - glucosidase and cobalt for producing fermentation products from starch |
| CN102834521B (zh) | 2010-03-30 | 2018-02-27 | 诺维信公司 | 用于增强来自发酵工艺副产物的方法 |
| CA2795806C (en) | 2010-04-14 | 2019-01-08 | Novozymes A/S | Polypeptides having glucoamylase activity and polynucleotides encoding same |
| CA2802083C (en) | 2010-06-11 | 2018-10-09 | Novozymes A/S | Enzymatic flour correction |
| US9308064B2 (en) | 2010-07-26 | 2016-04-12 | Johnson & Johnson Consumer Inc. | Devices and methods for collecting and analyzing fluid samples from the oral cavity |
| EP2601301A1 (en) | 2010-08-02 | 2013-06-12 | Novozymes North America, Inc. | Process of producing a fermentation product |
| CA2817224A1 (en) | 2010-11-19 | 2012-05-24 | Novozymes North America, Inc. | Processes of producing a fermentation product |
| CN103608460B (zh) | 2010-12-22 | 2017-08-29 | 诺维信北美公司 | 用于产生发酵产物的工艺 |
| CN103339260A (zh) | 2011-01-04 | 2013-10-02 | 诺维信公司 | 从含果胶和木素纤维素的材料产生生物气的方法 |
| US9677094B2 (en) | 2011-02-07 | 2017-06-13 | Novozymes A/S | Process of producing a fermentation product |
| WO2013000945A1 (en) | 2011-06-28 | 2013-01-03 | Novozymes A/S | Biogas from enzyme-treated bagasse |
| EP3421595B1 (en) | 2011-06-30 | 2020-10-07 | Novozymes A/S | Alpha-amylase-variants |
| MX337984B (es) | 2011-07-06 | 2016-03-30 | Novozymes As | Variantes de alfa amilasa y polinucleotidos que codifican la misma. |
| CN109022518A (zh) | 2011-07-22 | 2018-12-18 | 诺维信北美公司 | 用于预处理纤维素材料和改进其水解的方法 |
| EP2742350B1 (en) | 2011-08-08 | 2019-10-30 | The Coca-Cola Company | Cell lines comprising endogenous taste receptors and their uses |
| EP2766490B1 (en) | 2011-10-11 | 2017-04-12 | Novozymes North America, Inc. | Liquefaction process for producing fermentation products |
| IN2014CN04905A (enExample) | 2011-12-02 | 2015-09-18 | Novozymes As | |
| WO2013083801A2 (en) | 2011-12-09 | 2013-06-13 | Novozymes A/S | Biogas from substrates comprising animal manure and enzymes |
| WO2013096652A1 (en) | 2011-12-21 | 2013-06-27 | Novozymes, Inc. | Methods for determining the degradation of a biomass material |
| ES2935920T3 (es) | 2012-03-30 | 2023-03-13 | Novozymes North America Inc | Procesos de elaboración de productos de fermentación |
| CA2869047C (en) | 2012-03-30 | 2022-11-01 | Novozymes North America, Inc. | Processes of producing fermentation products |
| US9828595B2 (en) | 2012-08-17 | 2017-11-28 | Novozymes A/S | Thermostable asparaginase variants and polynucleotides encoding same |
| WO2014039773A1 (en) | 2012-09-07 | 2014-03-13 | Novozymes A/S | Glucoamylase variants and polynucleotides encoding same and uses thereof |
| CN119931852A (zh) * | 2012-12-11 | 2025-05-06 | 丹尼斯科美国公司 | 表达来自烟曲霉的葡糖淀粉酶的里氏木霉宿主细胞和其使用方法 |
| DK3022300T3 (en) | 2013-07-17 | 2018-10-22 | Novozymes As | : Pullulan chimeras and polynucleotides encoding them |
| US9951364B2 (en) | 2013-09-11 | 2018-04-24 | Novozymes A/S | Processes for producing fermentation products |
| EP3097192B1 (en) | 2014-01-22 | 2018-07-25 | Novozymes A/S | Pullulanase variants and polynucleotides encoding same |
| CA2937818C (en) | 2014-02-07 | 2023-08-01 | Novozymes A/S | Compositions for producing glucose syrups |
| WO2015143144A1 (en) | 2014-03-19 | 2015-09-24 | Novozymes A/S | Method for enhancing activity of an x143 polypeptide |
| WO2015157656A1 (en) | 2014-04-10 | 2015-10-15 | Novozymes A/S | Alpha-amylase variants and polynucleotides encoding same |
| EP4108087A1 (en) | 2014-07-08 | 2022-12-28 | Caravan Ingredients Inc. | Sugar-producing and texture-improving bakery methods and products formed therefrom |
| WO2016062875A2 (en) | 2014-10-23 | 2016-04-28 | Novozymes A/S | Glucoamylase variants and polynucleotides encoding same |
| BR112017011275A2 (pt) | 2014-12-01 | 2018-04-03 | Novozymes A/S | composição, e, processo para a produção de xarope de glicose. |
| US10676727B2 (en) | 2015-06-18 | 2020-06-09 | Novozymes A/S | Polypeptides having trehalase activity and the use thereof in process of producing fermentation products |
| CN108699572A (zh) | 2015-12-22 | 2018-10-23 | 诺维信公司 | 使用磷脂酶c增加发酵产物得率的方法 |
| US10067091B2 (en) | 2016-07-29 | 2018-09-04 | Saudi Arabian Oil Company | Integrated sediment and water analysis device and method |
| EP3526336A1 (en) | 2016-10-17 | 2019-08-21 | Novozymes A/S | Methods of reducing foam during ethanol fermentation |
| US10889836B2 (en) | 2016-11-23 | 2021-01-12 | Novozymes A/S | Yeast for ethanol production |
| BR112019021223A2 (pt) * | 2017-04-11 | 2020-04-28 | Novozymes A/S | variante de glucoamilase, métodos para aumentar a atividade de hidrólise de amido em bruto de uma glucoamilase e para produzir uma variante de glucoamilase, composição, uso de uma variante de glucoamilase, processos para produzir um produto de fermentação e para produzir um produto de xarope, polinucleotídeo codificando a variante de glucoamilase, construto de ácido nucleico, vetor de expressão, e, célula hospedeira. |
| KR102713243B1 (ko) * | 2017-05-05 | 2024-10-02 | 씨-렉타 게엠베하 | 글루코스 이소머라제 |
| AU2018275794A1 (en) | 2017-06-02 | 2019-12-05 | Novozymes A/S | Improved yeast for ethanol production |
| DK3645555T3 (da) | 2017-06-28 | 2022-03-07 | Novozymes As | Polypeptider med trehalaseaktivitet og polynukleotider, der koder for disse |
| CA3070281A1 (en) | 2017-08-08 | 2019-02-14 | Novozymes A/S | Polypeptides having trehalase activity and the use thereof in process of producing fermentation products |
| CN111164214A (zh) | 2017-09-15 | 2020-05-15 | 诺维信公司 | 用于改进动物饲料营养质量的酶共混物和方法 |
| US11326187B2 (en) | 2017-10-23 | 2022-05-10 | Novozymes A/S | Processes for producing a fermentation product |
| MX2020007914A (es) | 2018-01-29 | 2020-10-28 | Novozymes As | Microorganismos con uso de nitrogeno mejorado para produccion de etanol. |
| MX2020008309A (es) | 2018-02-15 | 2020-10-14 | Novozymes As | Levadura mejorada para produccion de etanol. |
| WO2019231944A2 (en) | 2018-05-31 | 2019-12-05 | Novozymes A/S | Processes for enhancing yeast growth and productivity |
| CA3104881A1 (en) | 2018-07-11 | 2020-01-16 | Novozymes A/S | Processes for producing fermentation products |
| CN112601818A (zh) | 2018-07-25 | 2021-04-02 | 诺维信公司 | 用于生产乙醇的表达酶的酵母 |
| WO2020076697A1 (en) | 2018-10-08 | 2020-04-16 | Novozymes A/S | Enzyme-expressing yeast for ethanol production |
| US11622751B2 (en) | 2018-12-19 | 2023-04-11 | Johnson & Johnson Consumer Inc. | Devices and methods for collecting saliva samples from the oral cavity |
| WO2020160126A1 (en) | 2019-01-31 | 2020-08-06 | Novozymes A/S | Polypeptides having xylanase activity and use thereof for improving the nutritional quality of animal feed |
| WO2020206058A1 (en) | 2019-04-02 | 2020-10-08 | Novozymes A/S | Process for producing a fermentation product |
| BR112022000351A2 (pt) | 2019-07-09 | 2022-05-10 | Dupont Nutrition Biosci Aps | Composições de enzima particuladas revestidas de gordura |
| MX2021015821A (es) | 2019-07-26 | 2022-02-03 | Novozymes As | Microorganismos con transporte de nitrogeno mejorado para la produccion de etanol. |
| EP4009807A1 (en) | 2019-08-05 | 2022-06-15 | Novozymes A/S | Enzyme blends and processes for producing a high protein feed ingredient from a whole stillage byproduct |
| MX2021015818A (es) | 2019-08-06 | 2022-02-03 | Novozymes As | Proteinas de fusion para mejorar la expresion de enzimas. |
| WO2021046073A1 (en) | 2019-09-05 | 2021-03-11 | Dupont Nutrition Biosciences Aps | Feed composition |
| EP4031661A1 (en) | 2019-09-16 | 2022-07-27 | Novozymes A/S | Polypeptides having beta-glucanase activity and polynucleotides encoding same |
| CA3158982A1 (en) | 2019-12-10 | 2021-06-17 | Monica TASSONE | Microorganism for improved pentose fermentation |
| MX2022006438A (es) | 2019-12-16 | 2022-06-22 | Novozymes As | Procesos para obtener productos de fermentacion. |
| WO2021163030A2 (en) | 2020-02-10 | 2021-08-19 | Novozymes A/S | Polypeptides having alpha-amylase activity and polynucleotides encoding same |
| AU2021370998A1 (en) | 2020-11-02 | 2023-05-25 | Novozymes A/S | Glucoamylase variants and polynucleotides encoding same |
| BR112023025624A2 (pt) | 2021-06-07 | 2024-02-27 | Novozymes As | Célula de levedura recombinante, célula hospedeira recombinante, composição, cocultura, métodos de produção de um derivado de uma célula hospedeira recombinante e de produção de um produto de fermentação, e, uso de uma célula hospedeira recombinante |
| EP4408186A1 (en) | 2021-09-27 | 2024-08-07 | International N&H Denmark ApS | Feed additive compositions and methods for using the same |
| CA3234874A1 (en) * | 2021-10-15 | 2023-04-20 | Martijn Scheffers | Glucoamylase variants and methods for use thereof |
| CN119546193A (zh) | 2022-05-17 | 2025-02-28 | 国际N&H丹麦有限公司 | 包含酶组合的饲料添加剂 |
| EP4638725A1 (en) | 2022-12-19 | 2025-10-29 | Novozymes A/S | Carbohydrate esterase family 3 (ce3) polypeptides having acetyl xylan esterase activity and polynucleotides encoding same |
| CN120283060A (zh) | 2022-12-19 | 2025-07-08 | 诺维信公司 | 用于使用纤维降解酶和工程化酵母生产发酵产物的工艺 |
| CN120380140A (zh) | 2022-12-19 | 2025-07-25 | 诺维信公司 | 具有阿魏酸酯酶和/或乙酰木聚糖酯酶活性的碳水化合物酯酶家族1（ce1）多肽和编码其的多核苷酸 |
| EP4638767A1 (en) | 2022-12-19 | 2025-10-29 | Novozymes A/S | Process for reducing syrup viscosity in the backend of a process for producing a fermentation product |
| WO2024137248A1 (en) | 2022-12-19 | 2024-06-27 | Novozymes A/S | Compositions comprising arabinofuranosidases and a xylanase, and use thereof for increasing hemicellulosic fiber solubilization |
| AU2024262752A1 (en) | 2023-04-28 | 2025-10-16 | International N&H Denmark Aps | Ruminant feed additive compositions |
| AU2024303961A1 (en) | 2023-06-13 | 2025-12-11 | Novozymes A/S | Processes for producing fermentation products using engineered yeast expressing a beta-xylosidase |
| WO2025128568A1 (en) | 2023-12-11 | 2025-06-19 | Novozymes A/S | Composition and use thereof for increasing hemicellulosic fiber solubilization |
| WO2026008449A2 (en) | 2024-07-04 | 2026-01-08 | Novozymes A/S | A process for producing a fermentation product and a concentrated protein co-product |
Family Cites Families (27)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4272326A (en) | 1980-01-24 | 1981-06-09 | Allied Chemical Corporation | Enhanced distillation of cyclohexanol from phenol with additional cyclohexanone feed |
| US4760025A (en) | 1984-05-29 | 1988-07-26 | Genencor, Inc. | Modified enzymes and methods for making same |
| US4683202A (en) | 1985-03-28 | 1987-07-28 | Cetus Corporation | Process for amplifying nucleic acid sequences |
| DK122686D0 (da) | 1986-03-17 | 1986-03-17 | Novo Industri As | Fremstilling af proteiner |
| JPS62272987A (ja) | 1986-05-22 | 1987-11-27 | Hitachi Plant Eng & Constr Co Ltd | ブドウ糖の製造方法 |
| DK463887D0 (da) | 1987-09-07 | 1987-09-07 | Novo Industri As | Gaerleader |
| JPH01191693A (ja) | 1988-01-25 | 1989-08-01 | Tdk Corp | デンプンの連続的糖化方法 |
| CA1333777C (en) | 1988-07-01 | 1995-01-03 | Randy M. Berka | Aspartic proteinase deficient filamentous fungi |
| JP2733330B2 (ja) | 1989-08-31 | 1998-03-30 | 日本食品化工株式会社 | 高純度澱粉糖の製造方法 |
| CA2038485A1 (en) | 1990-03-23 | 1991-09-24 | Donald K. Hadden | Nanofiltration process for making dextrose |
| ES2068586T5 (es) | 1990-05-09 | 2004-12-01 | Novozymes A/S | Una preparacion de celulasa que comprende una enzima endoglucanasa. |
| US5162210A (en) * | 1990-06-29 | 1992-11-10 | Iowa State University Research Foundation | Process for enzymatic hydrolysis of starch to glucose |
| US5231017A (en) | 1991-05-17 | 1993-07-27 | Solvay Enzymes, Inc. | Process for producing ethanol |
| US5665585A (en) * | 1992-09-03 | 1997-09-09 | Alko-Yhiot Oy | Recombinant production of glucoamylase P in trichoderma |
| US5605793A (en) | 1994-02-17 | 1997-02-25 | Affymax Technologies N.V. | Methods for in vitro recombination |
| DE4422198C2 (de) | 1994-06-24 | 1997-08-28 | Audi Ag | Verfahren zum Steuern der elektrischen Beheizung eines Katalysators |
| ATE317005T1 (de) | 1996-03-27 | 2006-02-15 | Novozymes As | Alkaline-phosphatase-defiziente, filamentöse pilze |
| CN1238009A (zh) * | 1996-07-24 | 1999-12-08 | 衣阿华州立大学研究基金会股份有限公司 | 提高葡糖淀粉酶pH最适点、底物专一性和热稳定性的蛋白质工程方法 |
| DK1032654T3 (da) | 1997-11-26 | 2009-05-11 | Novozymes As | Thermostabil glucoamylase |
| US6255084B1 (en) * | 1997-11-26 | 2001-07-03 | Novozymes A/S | Thermostable glucoamylase |
| US6352851B1 (en) * | 1998-07-15 | 2002-03-05 | Novozymes A/S | Glucoamylase variants |
| CN1329665A (zh) * | 1998-12-07 | 2002-01-02 | 诺维信公司 | 具有n末端延伸的葡糖淀粉酶 |
| US6329186B1 (en) * | 1998-12-07 | 2001-12-11 | Novozymes A/S | Glucoamylases with N-terminal extensions |
| AR029759A1 (es) * | 1999-07-09 | 2003-07-16 | Novozymes As | Variante de glucoamilasa original, una construccion de adn, un vector de expresion recombinante, una celula, un proceso para convertir almidon, uso de una variante de glucoamilasa para un proceso de fermentacion y metodo para mejorar la estabilidad termica. |
| US7226770B2 (en) * | 2000-04-28 | 2007-06-05 | Novozymes A/S | Lipolytic enzyme variant |
| MXPA06004463A (es) * | 2003-10-28 | 2006-06-27 | Novozymes North America Inc | Enzimas hibridas. |
| US7464662B2 (en) * | 2004-01-28 | 2008-12-16 | Tokyo Electron Limited | Compact, distributed inductive element for large scale inductively-coupled plasma sources |
-
2000
- 2000-07-07 AR ARP000103471A patent/AR029759A1/es active IP Right Grant
- 2000-07-07 CN CNA2009101412582A patent/CN101550410A/zh active Pending
- 2000-07-07 AU AU58057/00A patent/AU5805700A/en not_active Abandoned
- 2000-07-07 EP EP00943688A patent/EP1200566A2/en not_active Ceased
- 2000-07-07 JP JP2001509477A patent/JP2003504046A/ja active Pending
- 2000-07-07 EP EP08159171A patent/EP2009098A1/en not_active Withdrawn
- 2000-07-07 CA CA002374009A patent/CA2374009A1/en not_active Abandoned
- 2000-07-07 CN CNB008101329A patent/CN100510067C/zh not_active Expired - Fee Related
- 2000-07-07 WO PCT/DK2000/000373 patent/WO2001004273A2/en not_active Ceased
-
2003
- 2003-04-23 US US10/421,586 patent/US7354753B2/en not_active Expired - Fee Related
-
2008
- 2008-02-21 US US12/034,906 patent/US7927857B2/en not_active Expired - Fee Related
- 2008-12-11 AR ARP080105383A patent/AR069653A2/es unknown
-
2011
- 2011-03-01 US US13/037,751 patent/US8722369B2/en not_active Expired - Fee Related
Also Published As
| Publication number | Publication date |
|---|---|
| CA2374009A1 (en) | 2001-01-18 |
| WO2001004273A3 (en) | 2001-09-07 |
| JP2003504046A (ja) | 2003-02-04 |
| US7354753B2 (en) | 2008-04-08 |
| US20080213843A1 (en) | 2008-09-04 |
| US20040002142A1 (en) | 2004-01-01 |
| US7927857B2 (en) | 2011-04-19 |
| AR029759A1 (es) | 2003-07-16 |
| AR069653A2 (es) | 2010-02-10 |
| EP1200566A2 (en) | 2002-05-02 |
| US8722369B2 (en) | 2014-05-13 |
| CN100510067C (zh) | 2009-07-08 |
| AU5805700A (en) | 2001-01-30 |
| US20120208243A1 (en) | 2012-08-16 |
| WO2001004273A2 (en) | 2001-01-18 |
| CN1360630A (zh) | 2002-07-24 |
| EP2009098A1 (en) | 2008-12-31 |
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