DK2316929T3 - Maltogene alfa-amylasevarianter - Google Patents
Maltogene alfa-amylasevarianter Download PDFInfo
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- DK2316929T3 DK2316929T3 DK10181858.1T DK10181858T DK2316929T3 DK 2316929 T3 DK2316929 T3 DK 2316929T3 DK 10181858 T DK10181858 T DK 10181858T DK 2316929 T3 DK2316929 T3 DK 2316929T3
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- UYQJCPNSAVWAFU-UHFFFAOYSA-N malto-tetraose Natural products OC1C(O)C(OC(C(O)CO)C(O)C(O)C=O)OC(CO)C1OC1C(O)C(O)C(OC2C(C(O)C(O)C(CO)O2)O)C(CO)O1 UYQJCPNSAVWAFU-UHFFFAOYSA-N 0.000 description 1
- FJCUPROCOFFUSR-GMMZZHHDSA-N maltopentaose Chemical compound O[C@@H]1[C@@H](O)[C@@H](O[C@H]([C@H](O)CO)[C@H](O)[C@@H](O)C=O)O[C@H](CO)[C@H]1O[C@@H]1[C@H](O)[C@@H](O)[C@H](O[C@@H]2[C@@H]([C@@H](O)[C@H](O[C@@H]3[C@@H]([C@@H](O)[C@H](O)[C@@H](CO)O3)O)[C@@H](CO)O2)O)[C@@H](CO)O1 FJCUPROCOFFUSR-GMMZZHHDSA-N 0.000 description 1
- 235000012054 meals Nutrition 0.000 description 1
- 108010005942 methionylglycine Proteins 0.000 description 1
- 231100000219 mutagenic Toxicity 0.000 description 1
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- 229920001220 nitrocellulos Polymers 0.000 description 1
- 238000011330 nucleic acid test Methods 0.000 description 1
- 230000000269 nucleophilic effect Effects 0.000 description 1
- 229920001778 nylon Polymers 0.000 description 1
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- 235000019629 palatability Nutrition 0.000 description 1
- 230000036961 partial effect Effects 0.000 description 1
- 239000007793 ph indicator Substances 0.000 description 1
- 239000010452 phosphate Substances 0.000 description 1
- 239000008363 phosphate buffer Substances 0.000 description 1
- 239000004033 plastic Substances 0.000 description 1
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- 238000007747 plating Methods 0.000 description 1
- 229920002401 polyacrylamide Polymers 0.000 description 1
- 239000011148 porous material Substances 0.000 description 1
- 230000001376 precipitating effect Effects 0.000 description 1
- 238000001556 precipitation Methods 0.000 description 1
- 125000001500 prolyl group Chemical group [H]N1C([H])(C(=O)[*])C([H])([H])C([H])([H])C1([H])[H] 0.000 description 1
- 230000035484 reaction time Effects 0.000 description 1
- 230000009257 reactivity Effects 0.000 description 1
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- 230000006798 recombination Effects 0.000 description 1
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- 102220253319 rs1307934269 Human genes 0.000 description 1
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- 102220293525 rs370346756 Human genes 0.000 description 1
- 102220010822 rs397514616 Human genes 0.000 description 1
- 102200076366 rs57590980 Human genes 0.000 description 1
- 102220112195 rs72807847 Human genes 0.000 description 1
- 102200132327 rs769653717 Human genes 0.000 description 1
- 102200063467 rs869312822 Human genes 0.000 description 1
- 235000019515 salmon Nutrition 0.000 description 1
- 150000003839 salts Chemical class 0.000 description 1
- 238000000646 scanning calorimetry Methods 0.000 description 1
- 238000007423 screening assay Methods 0.000 description 1
- 238000002741 site-directed mutagenesis Methods 0.000 description 1
- 239000002002 slurry Substances 0.000 description 1
- 229910000029 sodium carbonate Inorganic materials 0.000 description 1
- 239000011780 sodium chloride Substances 0.000 description 1
- 239000001509 sodium citrate Substances 0.000 description 1
- NLJMYIDDQXHKNR-UHFFFAOYSA-K sodium citrate Chemical compound O.O.[Na+].[Na+].[Na+].[O-]C(=O)CC(O)(CC([O-])=O)C([O-])=O NLJMYIDDQXHKNR-UHFFFAOYSA-K 0.000 description 1
- 239000004289 sodium hydrogen sulphite Substances 0.000 description 1
- 235000010267 sodium hydrogen sulphite Nutrition 0.000 description 1
- 239000001488 sodium phosphate Substances 0.000 description 1
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- 230000007704 transition Effects 0.000 description 1
- RYFMWSXOAZQYPI-UHFFFAOYSA-K trisodium phosphate Chemical compound [Na+].[Na+].[Na+].[O-]P([O-])([O-])=O RYFMWSXOAZQYPI-UHFFFAOYSA-K 0.000 description 1
- 108010051110 tyrosyl-lysine Proteins 0.000 description 1
- 108010073969 valyllysine Proteins 0.000 description 1
- 108010009962 valyltyrosine Proteins 0.000 description 1
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Classifications
-
- 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
-
- 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
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2299/00—Coordinates from 3D structures of peptides, e.g. proteins or enzymes
Landscapes
- Life Sciences & Earth Sciences (AREA)
- Health & Medical Sciences (AREA)
- Engineering & Computer Science (AREA)
- Chemical & Material Sciences (AREA)
- Wood Science & Technology (AREA)
- Organic Chemistry (AREA)
- Biotechnology (AREA)
- Molecular Biology (AREA)
- Biomedical Technology (AREA)
- Zoology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Genetics & Genomics (AREA)
- Microbiology (AREA)
- Medicinal Chemistry (AREA)
- Biochemistry (AREA)
- General Engineering & Computer Science (AREA)
- General Health & Medical Sciences (AREA)
- Food Science & Technology (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Enzymes And Modification Thereof (AREA)
- Bakery Products And Manufacturing Methods Therefor (AREA)
- Detergent Compositions (AREA)
- Polysaccharides And Polysaccharide Derivatives (AREA)
- Noodles (AREA)
Claims (7)
1. Polypeptid, som: a) har maltogen alfa-amylaseaktivitet; b) udviser mindst 70% identitet med SEQ ID NO: 1; c) omfatter en aminosyremodifikation i sammenligning med SEQ ID NO: 1 i en position svarende til rest T288; og d) har en ændret pH-afhængig aktivitetsprofil i sammenligning med polypeptidet ifølge SEQ ID NO: 1.
2. Polypeptid ifølge krav 1, hvor modifikationen i sammenligning med SEQ ID NO: 1 omfatter T288E, T288K eller T288R.
3. Nukleinsyresekvens, som koder for polypeptidet ifølge et hvilket som helst af kravene 1-2, hvilken nukleinsyresekvens fortrinsvis er operativt forbundet til en eller flere kontrolsekvenser, der styrer ekspressionen af varianten i en egnet ekspressionsvært.
4. Rekombinant ekspressionsvektor, som omfatter nukleinsyresekvensen ifølge krav 3, en promotor og transskriptions- og translationsstopsignaler, og som fortrinsvis endvidere omfatter en selekterbar markør.
5. Transformeret værtscelle, som omfatter nukleinsyresekvensen ifølge krav 3 eller vektoren ifølge krav 4.
6. Fremgangsmåde til fremstilling af polypeptidet ifølge et hvilket som helst af kravene 1-2, hvilken fremgangsmåde omfatter: a) dyrkning af den transformerede værtscelle ifølge krav 6 under betingelser, som er befordrende for ekspression af varianten; og b) indvinding af varianten.
7. Fremgangsmåde til fremstilling af en dej eller et bagt produkt fremstillet af dej, hvilken fremgangsmåde omfatter tilsætning af polypeptidet ifølge et hvilket som helst af kravene 1-2 til dejen i en mængde, som er effektiv til at forsinke ældningen af brødet.
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| DK26998 | 1998-02-27 | ||
| EP99904736A EP1058724B1 (en) | 1998-02-27 | 1999-02-26 | Maltogenic alpha-amylase variants |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| DK2316929T3 true DK2316929T3 (da) | 2016-07-25 |
Family
ID=8091645
Family Applications (3)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| DK10181858.1T DK2316929T3 (da) | 1998-02-27 | 1999-02-26 | Maltogene alfa-amylasevarianter |
| DK99904736.8T DK1058724T3 (en) | 1998-02-27 | 1999-02-26 | Maltogene alpha-amylase varianter |
| DK10181883.9T DK2305799T3 (da) | 1998-02-27 | 1999-02-26 | Maltogene alfa-amylasevarianter |
Family Applications After (2)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| DK99904736.8T DK1058724T3 (en) | 1998-02-27 | 1999-02-26 | Maltogene alpha-amylase varianter |
| DK10181883.9T DK2305799T3 (da) | 1998-02-27 | 1999-02-26 | Maltogene alfa-amylasevarianter |
Country Status (14)
| Country | Link |
|---|---|
| US (1) | US6162628A (da) |
| EP (3) | EP1058724B1 (da) |
| JP (2) | JP4672864B2 (da) |
| CN (2) | CN1292028B (da) |
| AT (1) | ATE490312T1 (da) |
| AU (1) | AU757935B2 (da) |
| BR (1) | BRPI9908281B1 (da) |
| CA (2) | CA2321595C (da) |
| DE (1) | DE69942995D1 (da) |
| DK (3) | DK2316929T3 (da) |
| NZ (1) | NZ505820A (da) |
| RU (1) | RU2258739C2 (da) |
| TR (1) | TR200002498T2 (da) |
| WO (1) | WO1999043794A1 (da) |
Families Citing this family (221)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US6876932B1 (en) | 1998-02-27 | 2005-04-05 | Novozymes A/S | Maltogenic alpha-amylase variants |
| WO1999043793A1 (en) * | 1998-02-27 | 1999-09-02 | Novo Nordisk A/S | Amylolytic enzyme variants |
| US6940002B1 (en) * | 1998-11-12 | 2005-09-06 | Novozymes A/S | Transgenic plant expressing maltogenic alpha-amylase |
| AU1263100A (en) * | 1998-11-12 | 2000-06-05 | Novozymes A/S | Transgenic plant expressing maltogenic alpha-amylase |
| EP1214441A1 (en) * | 1999-09-01 | 2002-06-19 | Novozymes A/S | Maltogenic amylase-modified starch derivatives |
| AU6686100A (en) * | 1999-09-01 | 2001-03-26 | Novozymes A/S | Method for production of maltose and/or enzymatically modified starch |
| EP1294845A1 (en) * | 2000-06-30 | 2003-03-26 | The Procter & Gamble Company | Detergent compositions comprising a maltogenic alpha-amylase enzyme |
| CN100491525C (zh) | 2000-07-28 | 2009-05-27 | 汉高两合股份公司 | 从芽孢杆菌a7-7(dsm 12368)中提取的新型淀粉分解酶以及含有该新型淀粉分解酶的洗涤剂和清洗剂 |
| US20040166201A1 (en) * | 2001-09-18 | 2004-08-26 | Novozymes A/S | Enzymatic treatment of starchy food products for shortening the tempering step |
| ATE500749T1 (de) | 2001-09-18 | 2011-03-15 | Novozymes As | Enzymatische behandlung von stärkehaltigen lebensmittelprodukten zur verkürzung der temperierenzeit |
| US20040063184A1 (en) | 2002-09-26 | 2004-04-01 | Novozymes North America, Inc. | Fermentation processes and compositions |
| GB0305685D0 (en) * | 2003-03-12 | 2003-04-16 | Danisco | Enzyme |
| US20040253696A1 (en) | 2003-06-10 | 2004-12-16 | Novozymes North America, Inc. | Fermentation processes and compositions |
| DK1654355T3 (da) | 2003-06-13 | 2010-08-09 | Danisco | Pseudomonas polypeptidvarianter med ikke-maltogen exoamylaseaktivitet og deres anvendelse til fremstilling af fødevarer |
| US20070148287A1 (en) * | 2003-07-01 | 2007-06-28 | Novozymes A/S | Cgtase variants |
| CA2536376A1 (en) | 2003-07-07 | 2005-01-27 | Genencor International, Inc. | Exo-specific 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 |
| EP1664285A2 (en) | 2003-08-22 | 2006-06-07 | Novozymes A/S | Fungal alpha-amylase variants |
| EP1687419B1 (en) | 2003-10-28 | 2010-02-03 | Novozymes North America, Inc. | Hybrid enzymes |
| KR101336659B1 (ko) * | 2004-07-07 | 2013-12-04 | 다니스코 유에스 인크. | 폴리펩타이드 |
| WO2006012902A2 (en) | 2004-08-02 | 2006-02-09 | Novozymes A/S | Creation of diversity in polypeptides |
| EP1797179A1 (en) | 2004-08-02 | 2007-06-20 | Novozymes A/S | Maltogenic alpha-amylase variants |
| DK1794291T3 (da) * | 2004-09-24 | 2013-03-04 | Novozymes As | Fremgangsmåde til fremstilling af et dejbaseret produkt |
| CA2592083C (en) | 2004-12-22 | 2017-02-21 | Novozymes A/S | Hybrid enzymes consisting of an endo-amylase first amino acid sequence and a carbohydrate-binding module as second amino acid sequence |
| EP1831384B1 (en) | 2004-12-22 | 2015-08-12 | Novozymes A/S | Polypeptides having glucoamylase activity and polynucleotides encoding same |
| US8030050B2 (en) * | 2005-07-07 | 2011-10-04 | Danisco A/S | Modified amylases from Pseudomonas species |
| MX2008000374A (es) * | 2005-07-07 | 2008-03-07 | Danisco | Amilasa modificada de pseudomonas saccharophilia. |
| CN101405397A (zh) | 2006-03-22 | 2009-04-08 | 诺维信北美公司 | 发酵方法 |
| CN101528769B (zh) * | 2006-06-19 | 2015-09-30 | 杜邦营养生物科学有限公司 | 多肽 |
| EP3763220A1 (en) | 2007-02-13 | 2021-01-13 | Chr. Hansen A/S | Coagulation of milk |
| US8916369B2 (en) | 2007-03-14 | 2014-12-23 | Danisco Us Inc. | Trichoderma reesei α-amylase is a maltogenic enzyme |
| BRPI0809096A2 (pt) * | 2007-03-23 | 2014-09-09 | Danisco Us Inc Genecor Division | Produção aumentada de amilase através da adição n-terminal à proteína amilase madura |
| ES2393682T3 (es) * | 2007-03-26 | 2012-12-27 | De Staat Der Nederlanden, Vert. Door De Minister Van Vws | Vacunas mejoradas contra Bordotella pertussis basadas en mutantes de glicosiltransferasa LPS |
| DK3219804T3 (da) | 2007-04-24 | 2019-09-30 | Novozymes North America Inc | Afgiftning af forbehandlede lignocelluloseholdige materialer |
| WO2008148845A2 (en) | 2007-06-07 | 2008-12-11 | Novozymes A/S | Method of preparing a dough-based product |
| US9695549B2 (en) | 2007-09-03 | 2017-07-04 | Norozymes Als | Detoxifying and recycling of washing solution used in pretreatment of lignocellulose-containing materials |
| AU2009212526A1 (en) * | 2008-02-04 | 2009-08-13 | Danisco Us Inc. | TS23 alpha-amylase variants with altered properties |
| EP2103219A1 (en) | 2008-03-10 | 2009-09-23 | Novozymes A/S | Dough with fructan and fructan-degrading enzyme |
| US20110097779A1 (en) | 2008-06-23 | 2011-04-28 | Chee-Leong Soong | Processes for Producing Fermentation Products |
| DK2344650T3 (da) | 2008-09-30 | 2014-07-14 | Novozymes North America Inc | Forbedring af enzymatisk hydrolyse af forbehandlet lignocelluloseholdigt materiale med distillers dried grain med solubles (ddg/s) |
| CN102186965B (zh) | 2008-10-15 | 2014-10-08 | 诺维信公司 | 酿造方法 |
| EP2857515B1 (en) | 2008-11-20 | 2018-02-21 | Novozymes Inc. | Polypeptides having amylolytic enhancing activity and polynucleotides encoding same |
| WO2010078391A2 (en) | 2008-12-30 | 2010-07-08 | 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 |
| MX2012000322A (es) | 2009-07-17 | 2012-02-08 | Novozymes As | Metodo de analisis del decaimiento de la celulosa en la hidrolisis del material celulosico. |
| WO2011039324A1 (en) | 2009-09-30 | 2011-04-07 | Novozymes A/S | Steamed bread preparation methods and steamed bread improving compositions |
| US11999928B2 (en) | 2009-11-13 | 2024-06-04 | Novozymes A/S | Brewing method |
| WO2011058105A1 (en) * | 2009-11-13 | 2011-05-19 | Novozymes A/S | A brewing method |
| AU2010276468B2 (en) | 2009-11-30 | 2015-05-14 | Novozymes A/S | Polypeptides having glucoamylase activity and polynucleotides encoding same |
| ES2534066T3 (es) | 2009-11-30 | 2015-04-17 | Novozymes A/S | Polipéptidos que tienen actividad de glucoamilasa y polinucleótidos que codifican los mismos |
| MX2012006176A (es) | 2009-12-01 | 2012-06-25 | Novozymes North America Inc | Polipeptidos que tienen actividad de glucoamilasa y polinucleotidos que codifican los mismos. |
| 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 |
| WO2011100161A1 (en) | 2010-02-09 | 2011-08-18 | Novozymes North America, Inc. | Addition of alpha - glucosidase and cobalt for producing fermentation products from starch |
| EP3070171B1 (en) | 2010-03-30 | 2018-06-13 | Novozymes A/S | Process for enhancing by-products from fermentation processes |
| WO2011127802A1 (en) | 2010-04-14 | 2011-10-20 | Novozymes A/S | Polypeptides having glucoamylase activity and polynucleotides encoding same |
| AU2011263706B2 (en) | 2010-06-11 | 2014-07-24 | Novozymes A/S | Enzymatic flour correction |
| DK2595487T3 (da) | 2010-07-21 | 2019-01-07 | Novozymes As | Fremgangsmåde til fremstilling af et bagt produkt med øget aromastabilitet med katalase og phospholipase |
| CA2807312A1 (en) | 2010-08-02 | 2012-02-09 | Novozymes North America, Inc. | Process of producing a fermentation product |
| ES2649555T3 (es) | 2010-11-08 | 2018-01-12 | Novozymes A/S | Polipéptidos con actividad glucoamilasa y polinucleótidos que los codifican |
| ES2605235T3 (es) | 2010-11-08 | 2017-03-13 | Novozymes A/S | Polipéptidos que tienen actividad de glucoamilasa y polinucleótidos que codifican los mismos |
| CA2817224A1 (en) | 2010-11-19 | 2012-05-24 | Novozymes North America, Inc. | Processes of producing a fermentation product |
| US9816112B2 (en) | 2010-12-22 | 2017-11-14 | Novozymes A/S | Processes for producing fermentation products |
| US9677094B2 (en) | 2011-02-07 | 2017-06-13 | Novozymes A/S | Process of producing a fermentation product |
| EP2486799A1 (en) | 2011-02-14 | 2012-08-15 | DSM IP Assets B.V. | Method to produce cake with lipolytic enzyme and alpha-amylase |
| WO2012130969A1 (en) | 2011-03-29 | 2012-10-04 | Novozymes A/S | Process for production of a baked product |
| CA2840962C (en) | 2011-07-06 | 2021-04-13 | Novozymes A/S | Alpha amylase variants and polynucleotides encoding same |
| WO2013007820A1 (en) * | 2011-07-14 | 2013-01-17 | Dsm Ip Assets B.V. | Screening method |
| EP2734633B1 (en) | 2011-07-22 | 2019-05-01 | Novozymes North America, Inc. | Processes for pretreating cellulosic material and improving hydrolysis thereof |
| JP2014521356A (ja) | 2011-08-12 | 2014-08-28 | ノボザイムス アクティーゼルスカブ | マンガン添加による培養液粘度の低減 |
| EP2748188A4 (en) | 2011-08-26 | 2015-03-18 | Novozymes As | POLYPEPTIDES WITH GLUCCOAMYLASE ACTIVITY AND THESE CODING POLYNUCLEOTIDES |
| CN103930543B (zh) | 2011-09-06 | 2020-11-27 | 诺维信公司 | 葡糖淀粉酶变体和编码它们的多核苷酸 |
| CA2853000C (en) | 2011-10-11 | 2022-03-15 | Novozymes A/S | Glucoamylase variants and polynucleotides encoding same |
| CA2861678C (en) | 2011-10-11 | 2021-02-16 | Novozymes North America, Inc. | Processes for producing fermentation products |
| IN2014CN04905A (da) | 2011-12-02 | 2015-09-18 | Novozymes As | |
| EP2794899A1 (en) | 2011-12-21 | 2014-10-29 | Novozymes, Inc. | Methods for determining the degradation of a biomass material |
| EP2620496B1 (en) | 2012-01-30 | 2015-06-03 | DSM IP Assets B.V. | Alpha-amylase |
| ES2935920T3 (es) | 2012-03-30 | 2023-03-13 | Novozymes North America Inc | Procesos de elaboración de productos de fermentación |
| US9856498B2 (en) | 2012-03-30 | 2018-01-02 | Novozymes A/S | Processes of producing fermentation products |
| EP2847316A1 (en) | 2012-05-11 | 2015-03-18 | Novozymes A/S | A brewing method |
| US20150173402A1 (en) * | 2012-06-27 | 2015-06-25 | Novozymes A/S | Rice cooking method |
| EP2870256A1 (en) | 2012-07-06 | 2015-05-13 | Novozymes A/S | Inactivation of a production strain using a fatty acid |
| MX2015001969A (es) | 2012-08-17 | 2015-05-15 | Novozymes As | Variantes de asparaginasa termoestables y polinucleotidos que las codifican. |
| EP2914611B1 (en) | 2012-11-01 | 2018-08-29 | Novozymes A/S | Method for removal of dna |
| US9301533B2 (en) | 2013-03-01 | 2016-04-05 | Dsm Ip Assets B.V. | Alpha-amylase variants |
| EP2961281A2 (en) * | 2013-03-01 | 2016-01-06 | DSM IP Assets B.V. | Combination of an aplha-amylase and a g4-forming amylase |
| EP2961839B1 (en) | 2013-03-01 | 2018-11-07 | DSM IP Assets B.V. | Alpha-amylase variants |
| ES2674701T3 (es) | 2013-04-30 | 2018-07-03 | Novozymes A/S | Variantes de glucoamilasa y polinucleótidos que las codifican |
| US9963690B2 (en) | 2013-04-30 | 2018-05-08 | Novozymes A/S | Glucoamylase variants and polynucleotides encoding same |
| CN105209613A (zh) * | 2013-05-17 | 2015-12-30 | 诺维信公司 | 具有α淀粉酶活性的多肽 |
| WO2014194032A1 (en) | 2013-05-29 | 2014-12-04 | Danisco Us Inc. | Novel metalloproteases |
| EP3004342B1 (en) | 2013-05-29 | 2023-01-11 | Danisco US Inc. | Novel metalloproteases |
| US20160108388A1 (en) | 2013-05-29 | 2016-04-21 | Danisco Us Inc. | Novel metalloproteases |
| WO2014194034A2 (en) | 2013-05-29 | 2014-12-04 | Danisco Us Inc. | Novel metalloproteases |
| EP3022300B1 (en) | 2013-07-17 | 2018-07-11 | Novozymes A/S | Pullulanase chimeras and polynucleotides encoding same |
| CN105934518A (zh) | 2013-09-11 | 2016-09-07 | 诺维信公司 | 用于生产发酵产品的方法 |
| DK3080262T3 (da) | 2013-12-13 | 2019-05-06 | Danisco Us Inc | Serinproteaser af bacillus-arter |
| EP3910057A1 (en) | 2013-12-13 | 2021-11-17 | Danisco US Inc. | Serine proteases of the bacillus gibsonii-clade |
| KR20160099629A (ko) | 2013-12-16 | 2016-08-22 | 이 아이 듀폰 디 네모아 앤드 캄파니 | 점도 조절제로서의 폴리 알파-1,3-글루칸 에테르의 사용 |
| ES2835703T3 (es) | 2013-12-18 | 2021-06-23 | Nutrition & Biosciences Usa 4 Inc | Eteres de poli alfa-1,3-glucano catiónicos |
| EP3097192B1 (en) | 2014-01-22 | 2018-07-25 | Novozymes A/S | Pullulanase variants and polynucleotides encoding same |
| WO2015123323A1 (en) | 2014-02-14 | 2015-08-20 | E. I. Du Pont De Nemours And Company | Poly-alpha-1,3-1,6-glucans for viscosity modification |
| EP3116914B8 (en) | 2014-03-11 | 2021-04-21 | E. I. du Pont de Nemours and Company | Oxidized poly alpha-1,3-glucan as detergent builder |
| US20170096653A1 (en) | 2014-03-21 | 2017-04-06 | Danisco Us Inc. | Serine proteases of bacillus species |
| EP3129478B1 (en) | 2014-04-10 | 2019-03-27 | Novozymes A/S | Alpha-amylase variants and polynucleotides encoding same |
| EP3158043B1 (en) | 2014-06-19 | 2021-03-10 | Nutrition & Biosciences USA 4, Inc. | Compositions containing one or more poly alpha-1,3-glucan ether compounds |
| US9714403B2 (en) | 2014-06-19 | 2017-07-25 | E I Du Pont De Nemours And Company | Compositions containing one or more poly alpha-1,3-glucan ether compounds |
| DK3207129T3 (da) | 2014-10-17 | 2020-02-24 | Danisco Us Inc | Serinproteaser af bacillus-arten |
| WO2016062875A2 (en) | 2014-10-23 | 2016-04-28 | Novozymes A/S | Glucoamylase variants and polynucleotides encoding same |
| CN107148472A (zh) | 2014-10-27 | 2017-09-08 | 丹尼斯科美国公司 | 芽孢杆菌属物种的丝氨酸蛋白酶 |
| EP3957729A1 (en) | 2014-10-27 | 2022-02-23 | Danisco US Inc. | Serine proteases |
| EP3212783B1 (en) | 2014-10-27 | 2024-06-26 | Danisco US Inc. | Serine proteases |
| DK3212662T3 (da) | 2014-10-27 | 2020-07-20 | Danisco Us Inc | Serinproteaser |
| DK3212781T3 (da) | 2014-10-27 | 2019-12-16 | Danisco Us Inc | Serinproteaser |
| CN108064306B (zh) | 2014-12-23 | 2022-11-01 | 营养与生物科学美国4公司 | 酶促产生的纤维素 |
| CN104531636B (zh) * | 2015-01-19 | 2017-02-22 | 江南大学 | 一种麦芽糖淀粉酶的突变体及其制备方法 |
| CN107835855B (zh) | 2015-05-13 | 2022-05-13 | 丹尼斯科美国公司 | AprL-进化枝蛋白酶变体及其用途 |
| WO2016201069A1 (en) | 2015-06-09 | 2016-12-15 | Danisco Us Inc | Low-density enzyme-containing particles |
| FI3307427T3 (fi) | 2015-06-09 | 2023-11-09 | Danisco Us Inc | Osmoottiset puhkeavat kapselit |
| WO2016201040A1 (en) | 2015-06-09 | 2016-12-15 | Danisco Us Inc. | Water-triggered enzyme suspension |
| US11499146B2 (en) | 2015-06-17 | 2022-11-15 | Danisco Us Inc. | Bacillus gibsonii-clade serine proteases |
| EP4141113A1 (en) | 2015-11-05 | 2023-03-01 | Danisco US Inc | Paenibacillus sp. mannanases |
| JP7364330B2 (ja) | 2015-11-05 | 2023-10-18 | ダニスコ・ユーエス・インク | パエニバチルス(Paenibacillus)属種及びバチルス(Bacillus)属種のマンナナーゼ |
| JP7045313B2 (ja) | 2015-11-13 | 2022-03-31 | ニュートリション・アンド・バイオサイエンシーズ・ユーエスエー・フォー,インコーポレイテッド | 洗濯ケアおよび織物ケアにおいて使用するためのグルカン繊維組成物 |
| EP3374401B1 (en) | 2015-11-13 | 2022-04-06 | Nutrition & Biosciences USA 4, Inc. | Glucan fiber compositions for use in laundry care and fabric care |
| WO2017083226A1 (en) | 2015-11-13 | 2017-05-18 | E. I. Du Pont De Nemours And Company | Glucan fiber compositions for use in laundry care and fabric care |
| US11920170B2 (en) | 2015-12-09 | 2024-03-05 | Danisco Us Inc. | Alpha-amylase combinatorial variants |
| EP3390625B1 (en) | 2015-12-18 | 2023-09-06 | Danisco US Inc. | Polypeptides with endoglucanase activity and uses thereof |
| US10597645B2 (en) | 2015-12-22 | 2020-03-24 | Novozymes A/S | Process of extracting oil from thin stillage |
| JP2019518440A (ja) | 2016-05-03 | 2019-07-04 | ダニスコ・ユーエス・インク | プロテアーゼ変異体およびその使用 |
| CN109072213A (zh) | 2016-05-05 | 2018-12-21 | 丹尼斯科美国公司 | 蛋白酶变体及其用途 |
| WO2017210295A1 (en) | 2016-05-31 | 2017-12-07 | Danisco Us Inc. | Protease variants and uses thereof |
| EP3472313B1 (en) | 2016-06-17 | 2022-08-31 | Danisco US Inc. | Protease variants and uses thereof |
| US11653655B2 (en) | 2016-07-15 | 2023-05-23 | Novozymes A/S | Improving the rollability of flat breads |
| EP3535365A2 (en) | 2016-11-07 | 2019-09-11 | Danisco US Inc. | Laundry detergent composition |
| WO2018114940A1 (en) | 2016-12-21 | 2018-06-28 | Dsm Ip Assets B.V. | Lipolytic enzyme variants |
| WO2018114938A1 (en) | 2016-12-21 | 2018-06-28 | Dsm Ip Assets B.V. | Lipolytic enzyme variants |
| CN110312795B (zh) | 2016-12-21 | 2024-07-23 | 丹尼斯科美国公司 | 蛋白酶变体及其用途 |
| WO2018114941A1 (en) | 2016-12-21 | 2018-06-28 | Dsm Ip Assets B.V. | Lipolytic enzyme variants |
| WO2018114912A1 (en) | 2016-12-21 | 2018-06-28 | Dsm Ip Assets B.V. | Lipolytic enzyme variants |
| EP3559226B1 (en) | 2016-12-21 | 2023-01-04 | Danisco US Inc. | Bacillus gibsonii-clade serine proteases |
| BR112019017271A2 (pt) | 2017-02-20 | 2020-04-14 | Novozymes As | enzima lipolítica para uso em panificação |
| JP7231228B2 (ja) | 2017-02-24 | 2023-03-01 | ダニスコ・ユーエス・インク | バチルス・リケニフォルミスにおける増加したタンパク質産生のための組成物及び方法 |
| US12344847B2 (en) | 2017-03-13 | 2025-07-01 | Danstar Ferment Ag | Cell-associated heterologous food and/or feed enzymes |
| US11453871B2 (en) | 2017-03-15 | 2022-09-27 | Danisco Us Inc. | Trypsin-like serine proteases and uses thereof |
| EP3601515A1 (en) | 2017-03-31 | 2020-02-05 | Danisco US Inc. | Delayed release enzyme formulations for bleach-containing detergents |
| DK3641550T3 (da) | 2017-06-22 | 2021-07-05 | Novozymes As | Fremgangsmåde til forbedring af strækbarhed af dej under anvendelse af gamma-glutamyltranspeptidase |
| MX2019014556A (es) | 2017-06-30 | 2020-02-07 | Danisco Us Inc | Particulas que contienen enzimas de baja aglomeracion. |
| WO2019040412A1 (en) | 2017-08-23 | 2019-02-28 | Danisco Us Inc | METHODS AND COMPOSITIONS FOR EFFICIENT GENETIC MODIFICATION OF BACILLUS LICHENIFORMIS STRAINS |
| AU2018322748B2 (en) * | 2017-08-29 | 2024-05-02 | Novozymes A/S | Baker's yeast expressing anti-staling/freshness amylases |
| KR20200047668A (ko) | 2017-09-13 | 2020-05-07 | 다니스코 유에스 인크. | 바실러스에서 증가된 단백질 생산을 위한 변형된 5'-비번역 영역(utr) 서열 |
| CA3070730A1 (en) | 2017-09-15 | 2019-03-21 | Novozymes A/S | Enzyme blends and processes for improving the nutritional quality of animal feed |
| CA3075907A1 (en) | 2017-10-23 | 2019-05-02 | Novozymes A/S | Processes for reducing lactic acid in a biofuel fermentation system |
| EP3703661A1 (en) | 2017-11-02 | 2020-09-09 | Danisco US Inc. | Freezing point depressed solid matrix compositions for melt granulation of enzymes |
| US20200354708A1 (en) | 2017-11-29 | 2020-11-12 | Danisco Us Inc. | Subtilisin variants having improved stability |
| MX2020006518A (es) | 2017-12-21 | 2020-10-28 | Danisco Us Inc | Gránulos de fusión en caliente, que contienen enzimas, que comprenden un desecante termotolerante. |
| KR102715197B1 (ko) | 2018-01-03 | 2024-10-08 | 다니스코 유에스 인크. | 증가된 단백질 생산을 위한 돌연변이체 및 유전자 변형된 바실러스 세포 및 이의 방법 |
| US20200359656A1 (en) | 2018-02-08 | 2020-11-19 | Danisco Us Inc. | Thermally-resistant wax matrix particles for enzyme encapsulation |
| CN108486080B (zh) * | 2018-04-04 | 2020-06-09 | 江南大学 | 一种环糊精葡萄糖基转移酶及其制备方法 |
| US11944104B2 (en) | 2018-04-05 | 2024-04-02 | Dsm Ip Assets B.V. | Variant maltogenic alpha-amylase |
| EP3780960B1 (en) * | 2018-04-19 | 2026-01-14 | Novozymes A/S | Process for improving freshness of flat breads involving combination of maltogenic alpha amylase variants and flat bread dough premix |
| CN108841801A (zh) * | 2018-05-29 | 2018-11-20 | 江南大学 | 一种筛选酶中与酶活力相关的氨基酸残基的方法 |
| WO2019231944A2 (en) | 2018-05-31 | 2019-12-05 | Novozymes A/S | Processes for enhancing yeast growth and productivity |
| JP7489923B2 (ja) | 2018-06-04 | 2024-05-24 | ノボザイムス アクティーゼルスカブ | ベーキングに使用するための固形酵素物品 |
| US12171240B2 (en) | 2018-06-12 | 2024-12-24 | Novozymes A/S | Less added sugar in baked products |
| WO2019245704A1 (en) | 2018-06-19 | 2019-12-26 | Danisco Us Inc | Subtilisin variants |
| EP3799601A1 (en) | 2018-06-19 | 2021-04-07 | Danisco US Inc. | Subtilisin variants |
| US20210269833A1 (en) | 2018-07-11 | 2021-09-02 | Novozymes A/S | Processes for producing fermentation products |
| WO2020047215A1 (en) | 2018-08-30 | 2020-03-05 | Danisco Us Inc | Enzyme-containing granules |
| WO2020068486A1 (en) | 2018-09-27 | 2020-04-02 | Danisco Us Inc | Compositions for medical instrument cleaning |
| US12509672B2 (en) | 2018-11-28 | 2025-12-30 | Danisco Us Inc. | Subtilisin variants having improved stability |
| BR112021014873A2 (pt) | 2019-01-31 | 2021-10-05 | Novozymes A/S | Polipeptídeo, combinação de enzimas, polinucleotídeo, construto de ácido nucleico ou vetor de expressão recombinante, célula hospedeira recombinante, método de produção de um polipeptídeo, e, processo de produção de um produto de fermentação |
| US20220220419A1 (en) | 2019-05-24 | 2022-07-14 | Danisco Us Inc | Subtilisin variants and methods of use |
| CN110074386A (zh) * | 2019-05-30 | 2019-08-02 | 武汉轻工大学 | 一种抗老化挤压面筋及其制备方法 |
| US20220306968A1 (en) | 2019-06-06 | 2022-09-29 | Danisco Us Inc | Methods and compositions for cleaning |
| WO2021026201A1 (en) | 2019-08-05 | 2021-02-11 | Novozymes A/S | Enzyme blends and processes for producing a high protein feed ingredient from a whole stillage byproduct |
| EP4031560A1 (en) | 2019-08-14 | 2022-07-27 | Danisco US Inc | Compositions and methods for increased protein production in bacillus licheniformis |
| WO2021096857A1 (en) | 2019-11-11 | 2021-05-20 | Danisco Us Inc | Compositions and methods for enhanced protein production in bacillus cells |
| WO2021099457A1 (en) * | 2019-11-22 | 2021-05-27 | Novozymes A/S | Method for obtaining an oat-based product |
| CN114929022A (zh) | 2019-12-09 | 2022-08-19 | 诺维信公司 | 烘焙添加剂 |
| PY2084892A (es) | 2019-12-16 | 2022-07-26 | Novozymes As | Proceso para producir productos de fermentación |
| CN114945665A (zh) | 2020-01-15 | 2022-08-26 | 丹尼斯科美国公司 | 用于增强地衣芽孢杆菌中蛋白产生的组合物和方法 |
| CN113558081A (zh) | 2020-04-29 | 2021-10-29 | 诺维信公司 | 一种酶法减少烘焙产品中油脂使用量的方法 |
| EP4204553A1 (en) | 2020-08-27 | 2023-07-05 | Danisco US Inc. | Enzymes and enzyme compositions for cleaning |
| AU2021372822A1 (en) | 2020-11-02 | 2023-06-01 | Novozymes A/S | Baked and par-baked products with thermostable amg variants from penicillium |
| EP4284906A1 (en) | 2021-01-29 | 2023-12-06 | Danisco US Inc. | Compositions for cleaning and methods related thereto |
| WO2022178432A1 (en) | 2021-02-22 | 2022-08-25 | Danisco Us Inc. | Methods and compositions for producing proteins of interest in pigment deficient bacillus cells |
| EP4363565A1 (en) | 2021-06-30 | 2024-05-08 | Danisco US Inc. | Variant lipases and uses thereof |
| WO2023023644A1 (en) | 2021-08-20 | 2023-02-23 | Danisco Us Inc. | Polynucleotides encoding novel nucleases, compositions thereof and methods thereof for eliminating dna from protein preparations |
| US20240384205A1 (en) | 2021-09-03 | 2024-11-21 | Danisco Us Inc. | Laundry compositions for cleaning |
| CN117957318A (zh) | 2021-09-13 | 2024-04-30 | 丹尼斯科美国公司 | 含有生物活性物质的颗粒 |
| CN118679251A (zh) | 2021-12-16 | 2024-09-20 | 丹尼斯科美国公司 | 枯草杆菌蛋白酶变体和使用方法 |
| WO2023114939A2 (en) | 2021-12-16 | 2023-06-22 | Danisco Us Inc. | Subtilisin variants and methods of use |
| EP4448750A2 (en) | 2021-12-16 | 2024-10-23 | Danisco US Inc. | Subtilisin variants and uses thereof |
| CN118974227A (zh) | 2022-03-01 | 2024-11-15 | 丹尼斯科美国公司 | 用于清洁的酶和酶组合物 |
| EP4504928A1 (en) * | 2022-04-01 | 2025-02-12 | Danstar Ferment AG | N-terminus engineering of intracellular polypeptides expressed in recombinant eukaryotic host cells |
| WO2023250301A1 (en) | 2022-06-21 | 2023-12-28 | Danisco Us Inc. | Methods and compositions for cleaning comprising a polypeptide having thermolysin activity |
| WO2024050339A1 (en) | 2022-09-02 | 2024-03-07 | Danisco Us Inc. | Mannanase variants and methods of use |
| CN120112635A (zh) | 2022-09-02 | 2025-06-06 | 丹尼斯科美国公司 | 枯草杆菌蛋白酶变体及其相关方法 |
| EP4581119A1 (en) | 2022-09-02 | 2025-07-09 | Danisco US Inc. | Detergent compositions and methods related thereto |
| CN117106752A (zh) * | 2022-10-09 | 2023-11-24 | 山东舜丰生物科技有限公司 | 优化的Cas12蛋白及其应用 |
| CN120201929A (zh) | 2022-10-28 | 2025-06-24 | 诺维信公司 | 用于获得植物基食品配料的方法 |
| EP4615968A1 (en) | 2022-11-09 | 2025-09-17 | Danisco US Inc. | Subtilisin variants and methods of use |
| EP4626238A1 (en) | 2022-11-30 | 2025-10-08 | Novozymes A/S | Baking at low-ph with thermostable glucoamylase variants |
| WO2024137252A1 (en) | 2022-12-19 | 2024-06-27 | Novozymes A/S | Process for reducing syrup viscosity in the backend of a process for producing a fermentation product |
| EP4638724A1 (en) | 2022-12-19 | 2025-10-29 | Novozymes A/S | Carbohydrate esterase family 1 (ce1) polypeptides having ferulic acid esterase and/or acetyl xylan esterase activity and polynucleotides encoding same |
| JP2025541374A (ja) | 2022-12-19 | 2025-12-18 | ノボザイムス アクティーゼルスカブ | アラビノフラノシダーゼ及びキシラナーゼを含む組成物、並びにヘミセルロース系繊維の可溶化を増加させるためのその使用 |
| 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 |
| EP4638768A2 (en) | 2022-12-19 | 2025-10-29 | Novozymes A/S | Processes for producing fermentation products using fiber-degrading enzymes with engineered yeast |
| WO2024163584A1 (en) | 2023-02-01 | 2024-08-08 | Danisco Us Inc. | Subtilisin variants and methods of use |
| CN120712348A (zh) | 2023-03-06 | 2025-09-26 | 丹尼斯科美国公司 | 枯草杆菌蛋白酶变体和使用方法 |
| EP4680013A1 (en) | 2023-03-16 | 2026-01-21 | Nutrition & Biosciences USA 4, Inc. | Brevibacillus fermentate extracts for cleaning and malodor control and use thereof |
| WO2024243330A1 (en) | 2023-05-22 | 2024-11-28 | Caravan Ingredients Inc. | Baked goods enhancer and methods of making and using the same |
| WO2024258820A2 (en) | 2023-06-13 | 2024-12-19 | Novozymes A/S | Processes for producing fermentation products using engineered yeast expressing a beta-xylosidase |
| AU2024321426A1 (en) | 2023-08-09 | 2026-01-29 | Novozymes A/S | Methods for obtaining a plant-based food ingredient |
| CN121909283A (zh) | 2023-09-28 | 2026-04-21 | 丹尼斯科美国公司 | 具有改善的溶解度的变体角质酶及其用途 |
| CN121969733A (zh) | 2023-10-20 | 2026-05-01 | 丹尼斯科美国公司 | 枯草杆菌蛋白酶变体和使用方法 |
| 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 |
| WO2026024921A1 (en) | 2024-07-25 | 2026-01-29 | The Procter & Gamble Company | Detergent composition comprising a subtilisin variant and methods of use |
| WO2026050315A1 (en) | 2024-08-29 | 2026-03-05 | Danisco Us Inc. | Subtilisin variants and methods of use |
| CN120366271B (zh) * | 2025-06-26 | 2025-09-26 | 南京大学 | 麦芽糖淀粉酶突变体、生物材料、催化剂及应用 |
Family Cites Families (15)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US3912590A (en) | 1973-01-03 | 1975-10-14 | Novo Industri As | Procedure for liquefying starch |
| JPS57174089A (en) | 1981-04-20 | 1982-10-26 | Novo Industri As | Chain dividing enzyme product |
| DK135983D0 (da) * | 1983-03-25 | 1983-03-25 | Novo Industri As | Maltogen amylaseenzymprodukt og fremgangsmade til dets fremstilling og anvendelse |
| 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 |
| FI89076C (fi) | 1986-07-09 | 1993-08-10 | Novo Nordisk As | Alfa-amylasblandningar foer att oeverfoera staerkelse i vaetskeform och foerfarande foer oeverfoering av staerkelse i flytande form |
| JP2854009B2 (ja) | 1987-10-15 | 1999-02-03 | ノボ ノルディスク アクティーゼルスカブ | シクロデキストリングリコシルトランスフェラーゼ,その製法および使用 |
| DK0531372T4 (da) | 1990-05-09 | 2004-08-09 | Novozymes As | Cellulasepræparat omfattende et endoglucanaseenzym |
| AU657278B2 (en) | 1990-09-13 | 1995-03-09 | Novo Nordisk A/S | Lipase variants |
| KR100511499B1 (ko) * | 1995-02-03 | 2005-12-21 | 노보자임스 에이/에스 | 소정 특성을 가지는 알파-아밀라제 돌연변이체를 디자인하는 방법 |
| JP4057055B2 (ja) | 1995-04-21 | 2008-03-05 | ノボザイムス アクティーゼルスカブ | シクロマルトデキストリングルカノトランスフェラーゼ変異体 |
| ES2432519T3 (es) * | 1996-04-30 | 2013-12-04 | Novozymes A/S | Mutantes de alfa-amilasa |
| US5763385A (en) * | 1996-05-14 | 1998-06-09 | Genencor International, Inc. | Modified α-amylases having altered calcium binding properties |
| EP0887061A1 (en) * | 1997-06-28 | 1998-12-30 | The Procter & Gamble Company | Faecal collector |
-
1999
- 1999-02-26 CN CN99803315.4A patent/CN1292028B/zh not_active Expired - Lifetime
- 1999-02-26 BR BRPI9908281-0A patent/BRPI9908281B1/pt not_active IP Right Cessation
- 1999-02-26 EP EP99904736A patent/EP1058724B1/en not_active Expired - Lifetime
- 1999-02-26 DK DK10181858.1T patent/DK2316929T3/da active
- 1999-02-26 CA CA2321595A patent/CA2321595C/en not_active Expired - Lifetime
- 1999-02-26 EP EP10181883.9A patent/EP2305799B1/en not_active Expired - Lifetime
- 1999-02-26 CA CA2759907A patent/CA2759907A1/en not_active Abandoned
- 1999-02-26 JP JP2000533534A patent/JP4672864B2/ja not_active Expired - Lifetime
- 1999-02-26 DK DK99904736.8T patent/DK1058724T3/da active
- 1999-02-26 DE DE69942995T patent/DE69942995D1/de not_active Expired - Lifetime
- 1999-02-26 RU RU2000124530/13A patent/RU2258739C2/ru active
- 1999-02-26 WO PCT/DK1999/000088 patent/WO1999043794A1/en not_active Ceased
- 1999-02-26 AU AU25129/99A patent/AU757935B2/en not_active Expired
- 1999-02-26 DK DK10181883.9T patent/DK2305799T3/da active
- 1999-02-26 TR TR2000/02498T patent/TR200002498T2/xx unknown
- 1999-02-26 AT AT99904736T patent/ATE490312T1/de not_active IP Right Cessation
- 1999-02-26 EP EP10181858.1A patent/EP2316929B1/en not_active Expired - Lifetime
- 1999-02-26 NZ NZ505820A patent/NZ505820A/xx not_active IP Right Cessation
- 1999-02-26 CN CN201310296084.3A patent/CN103352033B/zh not_active Expired - Lifetime
- 1999-08-31 US US09/386,607 patent/US6162628A/en not_active Expired - Lifetime
-
2010
- 2010-04-01 JP JP2010085577A patent/JP5174077B2/ja not_active Expired - Lifetime
Also Published As
| Publication number | Publication date |
|---|---|
| JP2003521866A (ja) | 2003-07-22 |
| RU2258739C2 (ru) | 2005-08-20 |
| DK2305799T3 (da) | 2016-07-25 |
| NZ505820A (en) | 2002-10-25 |
| DK1058724T3 (en) | 2011-03-21 |
| EP2316929B1 (en) | 2016-04-27 |
| EP2305799A3 (en) | 2011-08-24 |
| TR200002498T2 (tr) | 2000-11-21 |
| AU757935B2 (en) | 2003-03-13 |
| CN1292028A (zh) | 2001-04-18 |
| CA2759907A1 (en) | 1999-09-02 |
| EP2316929A3 (en) | 2011-08-24 |
| AU2512999A (en) | 1999-09-15 |
| CN1292028B (zh) | 2013-08-14 |
| EP2316929A2 (en) | 2011-05-04 |
| CN103352033A (zh) | 2013-10-16 |
| JP5174077B2 (ja) | 2013-04-03 |
| ATE490312T1 (de) | 2010-12-15 |
| CA2321595C (en) | 2012-02-14 |
| EP1058724A1 (en) | 2000-12-13 |
| BRPI9908281B1 (pt) | 2015-06-02 |
| US6162628A (en) | 2000-12-19 |
| EP2305799A2 (en) | 2011-04-06 |
| DE69942995D1 (de) | 2011-01-13 |
| CN103352033B (zh) | 2016-05-11 |
| EP2305799B1 (en) | 2016-04-20 |
| CA2321595A1 (en) | 1999-09-02 |
| JP2010148525A (ja) | 2010-07-08 |
| WO1999043794A1 (en) | 1999-09-02 |
| BR9908281A (pt) | 2000-10-31 |
| JP4672864B2 (ja) | 2011-04-20 |
| EP1058724B1 (en) | 2010-12-01 |
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