NO324271B1 - Rekombinant heksoseoksidasepolypeptid (HOX), rekombinant DNA molekyl, fremgangsmate for fremstilling av HOX-polypeptidet og anvendelse av et slikt enzym i et naeringsprodukt. - Google Patents
Rekombinant heksoseoksidasepolypeptid (HOX), rekombinant DNA molekyl, fremgangsmate for fremstilling av HOX-polypeptidet og anvendelse av et slikt enzym i et naeringsprodukt. Download PDFInfo
- Publication number
- NO324271B1 NO324271B1 NO19975693A NO975693A NO324271B1 NO 324271 B1 NO324271 B1 NO 324271B1 NO 19975693 A NO19975693 A NO 19975693A NO 975693 A NO975693 A NO 975693A NO 324271 B1 NO324271 B1 NO 324271B1
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- Norway
- Prior art keywords
- polypeptide
- hexose oxidase
- hox
- recombinant
- cell
- Prior art date
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Classifications
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- 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
- C12N9/0004—Oxidoreductases (1.)
- C12N9/0006—Oxidoreductases (1.) acting on CH-OH groups as donors (1.1)
-
- A—HUMAN NECESSITIES
- A21—BAKING; EDIBLE DOUGHS
- A21D—TREATMENT, e.g. PRESERVATION, OF FLOUR OR DOUGH, e.g. BY ADDITION OF MATERIALS; BAKING; BAKERY PRODUCTS; PRESERVATION THEREOF
- 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
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23K—FODDER
- A23K30/00—Processes specially adapted for preservation of materials in order to produce animal feeding-stuffs
- A23K30/10—Processes specially adapted for preservation of materials in order to produce animal feeding-stuffs of green fodder
- A23K30/15—Processes specially adapted for preservation of materials in order to produce animal feeding-stuffs of green fodder using chemicals or microorganisms for ensilaging
- A23K30/18—Processes specially adapted for preservation of materials in order to produce animal feeding-stuffs of green fodder using chemicals or microorganisms for ensilaging using microorganisms or enzymes
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23L—FOODS, FOODSTUFFS, OR NON-ALCOHOLIC BEVERAGES, NOT COVERED BY SUBCLASSES A21D OR A23B-A23J; THEIR PREPARATION OR TREATMENT, e.g. COOKING, MODIFICATION OF NUTRITIVE QUALITIES, PHYSICAL TREATMENT; PRESERVATION OF FOODS OR FOODSTUFFS, IN GENERAL
- A23L27/00—Spices; Flavouring agents or condiments; Artificial sweetening agents; Table salts; Dietetic salt substitutes; Preparation or treatment thereof
- A23L27/20—Synthetic spices, flavouring agents or condiments
- A23L27/24—Synthetic spices, flavouring agents or condiments prepared by fermentation
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23L—FOODS, FOODSTUFFS, OR NON-ALCOHOLIC BEVERAGES, NOT COVERED BY SUBCLASSES A21D OR A23B-A23J; THEIR PREPARATION OR TREATMENT, e.g. COOKING, MODIFICATION OF NUTRITIVE QUALITIES, PHYSICAL TREATMENT; PRESERVATION OF FOODS OR FOODSTUFFS, IN GENERAL
- A23L3/00—Preservation of foods or foodstuffs, in general, e.g. pasteurising, sterilising, specially adapted for foods or foodstuffs
- A23L3/34—Preservation of foods or foodstuffs, in general, e.g. pasteurising, sterilising, specially adapted for foods or foodstuffs by treatment with chemicals
- A23L3/3454—Preservation of foods or foodstuffs, in general, e.g. pasteurising, sterilising, specially adapted for foods or foodstuffs by treatment with chemicals in the form of liquids or solids
- A23L3/3463—Organic compounds; Microorganisms; Enzymes
- A23L3/3571—Microorganisms; Enzymes
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K8/00—Cosmetics or similar toiletry preparations
- A61K8/18—Cosmetics or similar toiletry preparations characterised by the composition
- A61K8/30—Cosmetics or similar toiletry preparations characterised by the composition containing organic compounds
- A61K8/64—Proteins; Peptides; Derivatives or degradation products thereof
- A61K8/66—Enzymes
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61Q—SPECIFIC USE OF COSMETICS OR SIMILAR TOILETRY PREPARATIONS
- A61Q11/00—Preparations for care of the teeth, of the oral cavity or of dentures; Dentifrices, e.g. toothpastes; Mouth rinses
-
- 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
- C12P17/00—Preparation of heterocyclic carbon compounds with only O, N, S, Se or Te as ring hetero atoms
- C12P17/02—Oxygen as only ring hetero atoms
-
- 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
- C12P21/00—Preparation of peptides or proteins
- C12P21/02—Preparation of peptides or proteins having a known sequence of two or more amino acids, e.g. glutathione
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K2800/00—Properties of cosmetic compositions or active ingredients thereof or formulation aids used therein and process related aspects
- A61K2800/80—Process related aspects concerning the preparation of the cosmetic composition or the storage or application thereof
- A61K2800/86—Products or compounds obtained by genetic engineering
Landscapes
- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Health & Medical Sciences (AREA)
- Engineering & Computer Science (AREA)
- Organic Chemistry (AREA)
- Microbiology (AREA)
- Zoology (AREA)
- Wood Science & Technology (AREA)
- General Health & Medical Sciences (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Genetics & Genomics (AREA)
- Biotechnology (AREA)
- Chemical Kinetics & Catalysis (AREA)
- General Chemical & Material Sciences (AREA)
- Food Science & Technology (AREA)
- Polymers & Plastics (AREA)
- Biochemistry (AREA)
- General Engineering & Computer Science (AREA)
- Animal Behavior & Ethology (AREA)
- Molecular Biology (AREA)
- Veterinary Medicine (AREA)
- Public Health (AREA)
- Nutrition Science (AREA)
- Animal Husbandry (AREA)
- Birds (AREA)
- Oral & Maxillofacial Surgery (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Medicinal Chemistry (AREA)
- Biomedical Technology (AREA)
- Epidemiology (AREA)
- Enzymes And Modification Thereof (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Fodder In General (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Coloring Foods And Improving Nutritive Qualities (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Edible Seaweed (AREA)
Applications Claiming Priority (2)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
US47691095A | 1995-06-07 | 1995-06-07 | |
PCT/DK1996/000238 WO1996040935A1 (fr) | 1995-06-07 | 1996-06-04 | Hexose oxydase de recombinaison, procede de production et utilisation de cette enzyme |
Publications (3)
Publication Number | Publication Date |
---|---|
NO975693D0 NO975693D0 (no) | 1997-12-05 |
NO975693L NO975693L (no) | 1998-02-05 |
NO324271B1 true NO324271B1 (no) | 2007-09-17 |
Family
ID=23893752
Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
NO19975693A NO324271B1 (no) | 1995-06-07 | 1997-12-05 | Rekombinant heksoseoksidasepolypeptid (HOX), rekombinant DNA molekyl, fremgangsmate for fremstilling av HOX-polypeptidet og anvendelse av et slikt enzym i et naeringsprodukt. |
Country Status (21)
Country | Link |
---|---|
US (4) | US6251626B1 (fr) |
EP (2) | EP0832245B2 (fr) |
JP (1) | JP3917183B2 (fr) |
CN (1) | CN1266275C (fr) |
AR (2) | AR002301A1 (fr) |
AT (1) | ATE223489T1 (fr) |
AU (1) | AU705562B2 (fr) |
BR (1) | BRPI9609230B1 (fr) |
CA (1) | CA2224143C (fr) |
CO (1) | CO4520252A1 (fr) |
DE (1) | DE69623473T3 (fr) |
DK (1) | DK0832245T4 (fr) |
ES (1) | ES2182986T5 (fr) |
MY (1) | MY116524A (fr) |
NO (1) | NO324271B1 (fr) |
NZ (1) | NZ310420A (fr) |
PH (1) | PH11996053280B1 (fr) |
PL (1) | PL187218B1 (fr) |
TW (1) | TW438887B (fr) |
WO (1) | WO1996040935A1 (fr) |
ZA (1) | ZA964616B (fr) |
Families Citing this family (54)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
US6936289B2 (en) * | 1995-06-07 | 2005-08-30 | Danisco A/S | Method of improving the properties of a flour dough, a flour dough improving composition and improved food products |
GB9913050D0 (en) * | 1999-06-04 | 1999-08-04 | Danisco | Anti-fouling composition |
US8178090B2 (en) | 1995-06-07 | 2012-05-15 | Danisco A/S | Recombinant hexose oxidase |
US20050287250A1 (en) * | 1995-06-07 | 2005-12-29 | Danisco A/S | Method |
ATE223489T1 (de) | 1995-06-07 | 2002-09-15 | Danisco | Rekombinante hexose oxidase, verfahren zu deren herstellung und verwendung |
DE69604491T3 (de) | 1995-06-07 | 2008-09-25 | Danisco A/S | Methode zur verbesserung der eigenschaften von mehlteig, sowie zusammensetzung zur teigverbesserung und verbesserte nahrungsmittel |
US7745599B1 (en) | 1995-06-07 | 2010-06-29 | Danisco A/S | Hexose oxidase-encoding DNAs and methods of use thereof |
WO1998013478A2 (fr) * | 1996-09-04 | 1998-04-02 | Mogen International N.V. | Proteine antifongique, and codant ces proteines et hotes incorporant ces proteines |
CN100494363C (zh) * | 1997-12-22 | 2009-06-03 | 诺维信公司 | 糖氧化酶及其在焙烤中的用途 |
ES2188190T5 (es) | 1998-07-21 | 2007-11-16 | Danisco A/S | Producto alimentario. |
EP1008651A3 (fr) * | 1998-12-09 | 2000-06-21 | Bioteknologisk Institut | Séquences d'ADN modifiées, codantes pour l'hexose oxidase, et leur usage |
GB9927801D0 (en) * | 1999-11-24 | 2000-01-26 | Danisco | Method |
US7455990B2 (en) * | 1999-11-24 | 2008-11-25 | Danisco A/S | Method of extracting recombinant hexose oxidase |
DK1341422T3 (da) * | 2000-11-17 | 2007-05-29 | Danisco | Fremgangsmåde til hindring af Maillard-reaktion i födevarer |
US8163317B2 (en) | 2000-11-17 | 2012-04-24 | Danisco A/S | Method |
GB0028119D0 (en) | 2000-11-17 | 2001-01-03 | Danisco | Method |
WO2004039174A2 (fr) * | 2002-10-30 | 2004-05-13 | Danisco A/S | Procede |
AU2002227889A1 (en) * | 2001-01-31 | 2002-08-12 | Novozymes A/S | Oxidase free of catalase side activities |
WO2002074926A2 (fr) * | 2001-03-19 | 2002-09-26 | Cargill Incorporated | Myo-inositol oxygenase |
BRPI0209467B1 (pt) † | 2001-05-07 | 2015-03-17 | Kraft Foods Group Brands Llc | Processo para fabricar e preparar queijo e outros produtos lacticínios contendo ácido lactobiônico |
NZ528260A (en) | 2001-05-18 | 2005-09-30 | Danisco | Method of improving dough and bread quality with the addition of an enzyme that hydrolyses a glycolipid and a phospholipid and incapable of hydrolysing a triglyceride or monoglyceride |
US7550647B2 (en) | 2001-09-14 | 2009-06-23 | Advanced Bionutrition | Transfected shrimp as production systems for therapeutic proteins |
US20030077702A1 (en) * | 2001-10-23 | 2003-04-24 | Rajiv Shah | Method for formulating a glucose oxidase enzyme with a desired property or properties and a glucose oxidase enzyme with the desired property |
WO2003106333A1 (fr) * | 2002-06-17 | 2003-12-24 | Nutricepts, Inc. | Systeme de piegeage d'oxygene |
MXPA05007653A (es) | 2003-01-17 | 2005-09-30 | Danisco | Metodo. |
US7955814B2 (en) | 2003-01-17 | 2011-06-07 | Danisco A/S | Method |
US20050196766A1 (en) | 2003-12-24 | 2005-09-08 | Soe Jorn B. | Proteins |
US20040241283A1 (en) * | 2003-05-28 | 2004-12-02 | Domingues David J. | Method of preventing discoloration of dough, dough compositions, and dough products |
NO319624B1 (no) | 2003-09-15 | 2005-09-05 | Trouw Internat Bv | Fiskefôr for laksefisk i ferskvann og anvendelse av slikt fôr. |
US7906307B2 (en) | 2003-12-24 | 2011-03-15 | Danisco A/S | Variant lipid acyltransferases and methods of making |
US7718408B2 (en) | 2003-12-24 | 2010-05-18 | Danisco A/S | Method |
GB0716126D0 (en) | 2007-08-17 | 2007-09-26 | Danisco | Process |
PL1733037T3 (pl) | 2004-03-11 | 2015-04-30 | Genentech Inc | Sposób wytwarzania polipeptydów |
GB0405637D0 (en) | 2004-03-12 | 2004-04-21 | Danisco | Protein |
EP1740060A1 (fr) * | 2004-04-05 | 2007-01-10 | Danisco A/S | Procede enzymatique pour la reduction de l'acrylamide dans des produits alimentaires |
CA2576817C (fr) | 2004-05-03 | 2010-12-21 | Chr. Hansen A/S | Procede enzymatique pour l'obtention de rendements accrus de l'acide lactobionique |
WO2006008508A1 (fr) | 2004-07-16 | 2006-01-26 | Danisco A/S | Procede de demucilagination enzymatique |
US20090104165A1 (en) * | 2004-09-22 | 2009-04-23 | Bioworks, Inc. | Transgenic strains of trichoderma and their use in biocontrol |
EP2097518A1 (fr) * | 2006-12-20 | 2009-09-09 | Danisco US, INC., Genencor Division | Glucose oxydase stable au stockage |
BRPI0907750A2 (pt) * | 2008-02-04 | 2015-07-21 | Danisco Us Inc | Variantes de alfa-amilase de bacillus stearothermophilus e usos dos mesmos |
GB0901966D0 (en) | 2009-02-05 | 2009-03-11 | Danisco | Composition |
US9309414B2 (en) | 2009-02-06 | 2016-04-12 | Hempel A/S | Enzyme-based self-polishing coating compositions |
CN102341009A (zh) | 2009-03-20 | 2012-02-01 | 诺维信公司 | 营养饮料及其制造方法 |
EP2380957A1 (fr) | 2010-04-19 | 2011-10-26 | The Procter & Gamble Company | Composition détergente solide pour linge dotée d'un profile Ph dynamique au lavage |
US8999691B2 (en) * | 2010-06-29 | 2015-04-07 | Ultizyme International Ltd. | Glucose dehydrogenase |
EP2415863A1 (fr) | 2010-08-03 | 2012-02-08 | B.R.A.I.N. | Mutant de l'oxydase de glucose |
US8393514B2 (en) | 2010-09-30 | 2013-03-12 | Ethicon Endo-Surgery, Inc. | Selectively orientable implantable fastener cartridge |
JP6427110B2 (ja) | 2013-01-28 | 2018-11-21 | エフ ホフマン−ラ ロッシュ アクチェン ゲゼルシャフト | アスペルギルスニガー由来の新規グルコース酸化酵素 |
EP2796547B1 (fr) | 2013-04-24 | 2016-09-14 | Fraunhofer-Gesellschaft zur Förderung der angewandten Forschung e.V. | Nouveaux variants d'oxydase de glucose |
EP3979811A1 (fr) * | 2019-06-05 | 2022-04-13 | Danisco US Inc. | Procédés d'amélioration de la teneur en acides aminés de produits alimentaires pour animaux |
CN110790823B (zh) * | 2019-12-04 | 2021-02-09 | 江南大学 | 一种解淀粉芽孢杆菌产抑菌活性物质的方法 |
CA3182928A1 (fr) | 2020-05-29 | 2021-12-02 | Novozymes A/S | Procede de controle de boue dans un procede de fabrication de pate a papier ou de papier |
US20240279875A1 (en) | 2021-06-16 | 2024-08-22 | Novozymes A/S | Method for controlling slime in a pulp or paper making process |
CN113667613A (zh) * | 2021-06-24 | 2021-11-19 | 浙江新银象生物工程有限公司 | 一株重组毕赤酵母工程菌及其应用 |
Family Cites Families (53)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
DE1050703B (de) | 1959-02-19 | Koninklijke Industrieele Maatschappij, Voorhen Noury &. van der Lande N. V., Deventer (Niederlande) | Verfahren zur Verbesserung der Backfähigkeit von Mehl oder Teig | |
US2783150A (en) | 1952-09-25 | 1957-02-26 | Pfizer & Co C | Treatment of flour with glucose oxidase |
CH461935A (fr) | 1966-05-03 | 1968-08-31 | Menzi Robert | Procédé de fabrication de pâtes alimentaires séchées |
JPS4816612B1 (fr) * | 1970-12-29 | 1973-05-23 | ||
JPS5850719B2 (ja) | 1978-10-18 | 1983-11-11 | 協和醗酵工業株式会社 | トリグリセライドの定量方法 |
JPS6185158A (ja) | 1984-10-03 | 1986-04-30 | Kiichi Kusumoto | 体質改善食品 |
US5190877A (en) * | 1987-09-03 | 1993-03-02 | Gist-Brocades N.V. | Saccharomyces strains for maltose fermentation |
ES2032939T5 (es) | 1987-12-21 | 2000-06-01 | Dsm Nv | Un metodo para mejorar una masa de harina. |
FI84970C (fi) | 1988-04-22 | 1992-02-25 | Suomen Sokeri Oy | Foerfarande foer foerbaettring av degens egenskaper och broedets kvalitet. |
US5094951A (en) | 1988-06-21 | 1992-03-10 | Chiron Corporation | Production of glucose oxidase in recombinant systems |
JPH02224143A (ja) | 1989-02-27 | 1990-09-06 | Fujitsu Ltd | テストプログラム作成処理装置 |
GB8906837D0 (en) * | 1989-03-23 | 1989-05-10 | Unilever Plc | Bread improvers |
JP2687247B2 (ja) | 1989-11-22 | 1997-12-08 | オリエンタル酵母工業株式会社 | パン類の製造法 |
NL9001388A (nl) * | 1990-06-19 | 1992-01-16 | Unilever Nv | Recombinant dna, cel die daarvan afgeleid dna bevat, enzym waarvoor het recombinant dna codeert en toepassingen daarvan. |
JP2954673B2 (ja) | 1990-07-26 | 1999-09-27 | オリエンタル酵母工業株式会社 | 製パン改良剤及びそれを用いる製パン方法 |
JP3006085B2 (ja) | 1990-11-30 | 2000-02-07 | オリエンタル酵母工業株式会社 | 製パン改良剤及びそれを用いる製パン法 |
EP0468731A1 (fr) | 1990-07-26 | 1992-01-29 | Oriental Yeast Co., Ltd. | Composition d'amélioration du pain et méthode de production de pain |
US5059430A (en) | 1990-09-12 | 1991-10-22 | Enzyme Bio-Systems Ltd. | Enzyme composition for retarding staling of baked goods |
JPH04207146A (ja) | 1990-11-30 | 1992-07-29 | Wakayama Pref Gov Nousanbutsu Kako Kenkyusho | 果実ピューレーを含むパンの製造法 |
JPH04207145A (ja) | 1990-11-30 | 1992-07-29 | Eguchi Koichiro | パン |
US5318785A (en) | 1991-11-26 | 1994-06-07 | Elf Atochem North America, Inc. | Benzoyl peroxide to improve the performance of oxidants in breadmaking |
JP3237902B2 (ja) | 1992-06-26 | 2001-12-10 | 株式会社竹中工務店 | 繊維補強材及びそれを用いた構造用材料 |
ES2087646T3 (es) | 1992-07-27 | 1996-07-16 | Gist Brocades Nv | Producto enzimatico y metodo para mejorar la calidad del pan. |
DE4301904A1 (de) * | 1992-08-07 | 1994-02-10 | Boehringer Mannheim Gmbh | Hypoglycosylierte recombinante Glucoseoxidase |
DK104592D0 (da) | 1992-08-21 | 1992-08-21 | Novo Nordisk As | Fremgangsmaade |
DE69329785D1 (de) | 1992-09-17 | 2001-02-01 | Dsm Nv | Hefederivate und Verfahren zum Verbessern der Brotqualität |
JP2980507B2 (ja) | 1993-02-17 | 1999-11-22 | オルガノ株式会社 | テクスチャーの改良された小麦粉製品およびその製造方法 |
AU6926794A (en) | 1993-07-06 | 1995-02-06 | Quest International B.V. | Enzyme containing particles |
EP0650669B1 (fr) | 1993-10-29 | 2002-01-09 | Dsm N.V. | Compositions d'agent améliorant pour la cuisson |
WO1995012996A1 (fr) | 1993-11-12 | 1995-05-18 | Ajit Khubani | Fer a friser pourvu d'un element de guidage de rouleaux a cheveux |
JP3407083B2 (ja) | 1994-04-04 | 2003-05-19 | 株式会社ベルリッチ | パン類の製造方法 |
WO1995029996A1 (fr) | 1994-05-03 | 1995-11-09 | Novo Nordisk A/S | Glucose-oxydase alcaline |
DE69501228T2 (de) | 1994-05-11 | 1998-05-07 | Amano Pharma Co Ltd | Ascorbatoxidase, dafür kodierendes Gen, Verfahren zu ihrer Herstellung und dieselbe verwendende Reagens-Zusammensetzung |
JPH07316612A (ja) | 1994-05-20 | 1995-12-05 | Fukuda Metal Foil & Powder Co Ltd | 消耗電極棒 |
EP0687414B1 (fr) | 1994-06-17 | 2000-11-08 | Dsm N.V. | Composition d'amélioration du pain |
AU684658B2 (en) | 1994-09-07 | 1997-12-18 | Gist-Brocades B.V. | Bread dough containing hemicellulase and sulfhydryl oxidase and method of preparing same |
GB0112226D0 (en) | 2001-05-18 | 2001-07-11 | Danisco | Method of improving dough and bread quality |
DE69604491T3 (de) * | 1995-06-07 | 2008-09-25 | Danisco A/S | Methode zur verbesserung der eigenschaften von mehlteig, sowie zusammensetzung zur teigverbesserung und verbesserte nahrungsmittel |
ATE223489T1 (de) | 1995-06-07 | 2002-09-15 | Danisco | Rekombinante hexose oxidase, verfahren zu deren herstellung und verwendung |
CA2234620A1 (fr) | 1995-12-20 | 1997-06-26 | Novo Nordisk A/S | Utilisation d'une pyranose-oxydase en boulangerie |
EP0973399B1 (fr) | 1997-04-09 | 2002-07-17 | Danisco A/S | Procede ameliore de preparation de pates et de produits obtenus a partir de ces pates en utilisant une glycerine oxydase |
JP3382837B2 (ja) | 1998-01-27 | 2003-03-04 | 三菱重工業株式会社 | 排煙脱硫装置の空気吹込み装置 |
JPH11207146A (ja) | 1997-11-17 | 1999-08-03 | Japan Organo Co Ltd | 排煙脱硫排水からの石膏回収方法 |
JPH11164127A (ja) | 1997-11-28 | 1999-06-18 | Canon Inc | 画像処理装置及びその方法並びにメモリ媒体 |
CN100494363C (zh) | 1997-12-22 | 2009-06-03 | 诺维信公司 | 糖氧化酶及其在焙烤中的用途 |
NZ511340A (en) | 1998-11-27 | 2003-07-25 | Novozymes As | Lipolytic enzyme variants |
US7455990B2 (en) * | 1999-11-24 | 2008-11-25 | Danisco A/S | Method of extracting recombinant hexose oxidase |
GB2358784B (en) | 1999-12-03 | 2004-06-30 | Danisco | Method of improving dough and bread quality |
JP2003515332A (ja) | 1999-12-03 | 2003-05-07 | ダニスコ アクティーゼルスカブ | 生地およびパンの品質を改良する方法 |
EP2119773A1 (fr) | 2000-06-26 | 2009-11-18 | Novozymes A/S | Enzyme lipolytique des souches fusarium ou acremonium |
WO2002003805A1 (fr) | 2000-07-06 | 2002-01-17 | Novozymes A/S | Procede de preparation d'une pate ou d'un produit de cuisson a partir d'une pate avec apport d'enzymes lipolytiques |
KR20030078065A (ko) | 2001-02-21 | 2003-10-04 | 노보자임스 에이/에스 | 녹말 식품의 제법 |
EP1404827A2 (fr) | 2001-02-23 | 2004-04-07 | Novozymes A/S | Genes d'enzyme lipolytique |
-
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