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 PDF

Info

Publication number: NO324271B1
Authority: NO; Norway
Prior art keywords: polypeptide; hexose oxidase; hox; recombinant; cell
Prior art date: 1995-06-07

Application number

NO19975693A

Other languages

English (en)

Norwegian (no)

Other versions

NO975693L (no

NO975693D0 (no

Inventor

Peter Stougaard

Ole Cai Hansen

Original Assignee

Danisco

Priority date (The priority date is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the date listed.)

1995-06-07

Filing date

1997-12-05

Publication date

2007-09-17

Family has litigation

First worldwide family litigation filed litigation Critical https://patents.darts-ip.com/?family=23893752&utm_source=***_patent&utm_medium=platform_link&utm_campaign=public_patent_search&patent=NO324271(B1) "Global patent litigation dataset” by Darts-ip is licensed under a Creative Commons Attribution 4.0 International License.

1997-12-05 Application filed by Danisco filed Critical Danisco

1997-12-05 Publication of NO975693D0 publication Critical patent/NO975693D0/no

1998-02-05 Publication of NO975693L publication Critical patent/NO975693L/no

2007-09-17 Publication of NO324271B1 publication Critical patent/NO324271B1/no

Links

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- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
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- C12N9/0006—Oxidoreductases (1.) acting on CH-OH groups as donors (1.1)
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- 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
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- 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
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- 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
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- 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

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Life Sciences & Earth Sciences (AREA)
Chemical & Material Sciences (AREA)
Health & Medical Sciences (AREA)
Engineering & Computer Science (AREA)
Microbiology (AREA)
Organic Chemistry (AREA)
Zoology (AREA)
Wood Science & Technology (AREA)
General Health & Medical Sciences (AREA)
Chemical Kinetics & Catalysis (AREA)
General Chemical & Material Sciences (AREA)
Bioinformatics & Cheminformatics (AREA)
Polymers & Plastics (AREA)
Genetics & Genomics (AREA)
Biotechnology (AREA)
Food Science & Technology (AREA)
Biochemistry (AREA)
General Engineering & Computer Science (AREA)
Nutrition Science (AREA)
Animal Behavior & Ethology (AREA)
Veterinary Medicine (AREA)
Molecular Biology (AREA)
Public Health (AREA)
Medicinal Chemistry (AREA)
Birds (AREA)
Biomedical Technology (AREA)
Animal Husbandry (AREA)
Oral & Maxillofacial Surgery (AREA)
Proteomics, Peptides & Aminoacids (AREA)
Epidemiology (AREA)
Enzymes And Modification Thereof (AREA)
Micro-Organisms Or Cultivation Processes Thereof (AREA)
Fodder In General (AREA)
Coloring Foods And Improving Nutritive Qualities (AREA)
Preparation Of Compounds By Using Micro-Organisms (AREA)
Edible Seaweed (AREA)
Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)

NO19975693A 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. NO324271B1 (no)

Applications Claiming Priority (2)

Application Number	Priority Date	Filing Date	Title
US47691095A	1995-06-07	1995-06-07
PCT/DK1996/000238 WO1996040935A1 (en)	1995-06-07	1996-06-04	Recombinant hexose oxidase, a method of producing same and use of such 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 (es)
EP (2)	EP0832245B2 (es)
JP (1)	JP3917183B2 (es)
CN (1)	CN1266275C (es)
AR (2)	AR002301A1 (es)
AT (1)	ATE223489T1 (es)
AU (1)	AU705562B2 (es)
BR (1)	BRPI9609230B1 (es)
CA (1)	CA2224143C (es)
CO (1)	CO4520252A1 (es)
DE (1)	DE69623473T3 (es)
DK (1)	DK0832245T4 (es)
ES (1)	ES2182986T5 (es)
MY (1)	MY116524A (es)
NO (1)	NO324271B1 (es)
NZ (1)	NZ310420A (es)
PH (1)	PH11996053280B1 (es)
PL (1)	PL187218B1 (es)
TW (1)	TW438887B (es)
WO (1)	WO1996040935A1 (es)
ZA (1)	ZA964616B (es)

Families Citing this family (54)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
US7745599B1 (en)	1995-06-07	2010-06-29	Danisco A/S	Hexose oxidase-encoding DNAs and methods of use thereof
PL184045B1 (pl)	1995-06-07	2002-08-30	Danisco	Sposób polepszania reologicznych właściwości ciasta z mąki oraz jakości wytworzonego z ciasta wyrobu gotowego
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
GB9913050D0 (en) *	1999-06-04	1999-08-04	Danisco	Anti-fouling composition
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
PL187218B1 (pl) *	1995-06-07	2004-06-30	Danisco	Sposób wytwarzania polipeptydu, polipeptyd pochodzący z gatunku alg morskich, rekombinowana cząsteczka DNA, komórka drobnoustroju, sposób wytwarzaniaproduktu spożywczego, sposób wytwarzania paszy zwierzęcej, sposób redukowania zawartości cukru w produkcie spożywczym, sposób wytwarzania produktu, sposób wytwarzania produktu pieczonego z ciasta, kompozycja polepszająca ciasto, sposób analizowania zawartości cukru w próbce, sposób wytwarzania laktonu
JP2001502525A (ja) *	1996-09-04	2001-02-27	モーヘンインターナショナルエヌ．ブイ．	抗真菌タンパク質、これをコードするこのｄｎａ、およびこのｄｎａを組込む宿主
JP4417550B2 (ja) *	1997-12-22	2010-02-17	ノボザイムスアクティーゼルスカブ	糖質酸化酵素およびベーキングにおけるその使用
AU752215B2 (en)	1998-07-21	2002-09-12	Dupont Nutrition Biosciences Aps	Foodstuff
EP1008651A3 (en) *	1998-12-09	2000-06-21	Bioteknologisk Institut	Modified DNA sequence coding for hexose oxidase and use hereof
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
CN1230101C (zh) *	2000-11-17	2005-12-07	丹尼斯科有限公司	方法
GB0028119D0 (en)	2000-11-17	2001-01-03	Danisco	Method
WO2004039174A2 (en) *	2002-10-30	2004-05-13	Danisco A/S	A method of preventing acrylamide formation in a foodstuff
US8163317B2 (en)	2000-11-17	2012-04-24	Danisco A/S	Method
WO2002061068A2 (en) *	2001-01-31	2002-08-08	Novozymes A/S	Oxidase free of catalase side activities
JP2004536577A (ja) *	2001-03-19	2004-12-09	カーギル，インコーポレーテッド	ミオイノシトールオキシゲナーゼ
ES2290290T5 (es) †	2001-05-07	2016-11-22	Kraft Foods Group Brands Llc	Procedimiento de fabricación de quesos y productos de los mismos
ATE362315T1 (de)	2001-05-18	2007-06-15	Danisco	Verfahren zur herstellung von teig mit einem enzym
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 (en) *	2002-06-17	2003-12-24	Nutricepts, Inc.	Oxygen scavenging system
US7955814B2 (en)	2003-01-17	2011-06-07	Danisco A/S	Method
US20050196766A1 (en)	2003-12-24	2005-09-08	Soe Jorn B.	Proteins
MXPA05007654A (es)	2003-01-17	2005-09-30	Danisco	Metodo.
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
CN1954074B (zh)	2004-03-11	2011-08-24	健泰科生物技术公司	多肽的制备方法
GB0405637D0 (en)	2004-03-12	2004-04-21	Danisco	Protein
WO2005096838A1 (en) *	2004-04-05	2005-10-20	Danisco A/S	Enzymatic process for acrylamide reduction in foodstuffs
EP1753297B1 (en)	2004-05-03	2017-09-27	Novozymes A/S	Enzymatic process for obtaining increased yield of lactobionic acid
EP2267108A1 (en)	2004-07-16	2010-12-29	Danisco A/S	Enzymatic oil-degumming method
EP1802740A4 (en) *	2004-09-22	2008-02-27	Bioworks Inc	TRANSGENIC STRAINS OF TRICHODERMA AND THEIR USE IN BIOLOGICAL CONTROL
CN101558153A (zh) *	2006-12-20	2009-10-14	丹尼斯科美国公司	稳定储藏的葡糖氧化酶
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 (en)	2010-04-19	2011-10-26	The Procter & Gamble Company	Solid laundry detergent composition having a dynamic in-wash ph profile
KR20130038914A (ko) *	2010-06-29	2013-04-18	유겐가이샤 얼티자임 인터내셔널	글루코스 탈수소효소
EP2415863A1 (en)	2010-08-03	2012-02-08	B.R.A.I.N.	Mutant glucose oxidase
US8757465B2 (en)	2010-09-30	2014-06-24	Ethicon Endo-Surgery, Inc.	Fastener system comprising a retention matrix and an alignment matrix
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 (en)	2013-04-24	2016-09-14	Fraunhofer-Gesellschaft zur Förderung der angewandten Forschung e.V.	Novel glucose oxidase variants
US20220232855A1 (en) *	2019-06-05	2022-07-28	Danisco Us Inc	Methods for improving the amino acid content of animal feed products
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
WO2021239950A1 (en)	2020-05-29	2021-12-02	Novozymes A/S	Method for controlling slime in a pulp or paper making process
WO2022263553A1 (en)	2021-06-16	2022-12-22	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)

* Cited by examiner, † Cited by third party
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 (es)	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.
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
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
EP0468731A1 (en)	1990-07-26	1992-01-29	Oriental Yeast Co., Ltd.	Bread improver and method of producing bread
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 (en) *	1993-10-29	2002-01-09	Dsm N.V.	Baking improver compositions
WO1995012996A1 (en)	1993-11-12	1995-05-18	Ajit Khubani	Hair curling iron with hair roller guide
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
US5741688A (en)	1994-05-03	1998-04-21	Novo Nordisk A/S	Alkaline glucose oxidase obtained from cladosporium oxysporum
EP0682116B1 (en)	1994-05-11	1997-12-17	Amano Pharmaceutical Co., Ltd.	Ascorbate oxidase, gene encoding the same, process for producing the same, and reagent composition using the same
JPH07316612A (ja)	1994-05-20	1995-12-05	Fukuda Metal Foil & Powder Co Ltd	消耗電極棒
DE69519331D1 (de) *	1994-06-17	2000-12-14	Dsm Nv	Zusammensetzung zur Brotverbesserung
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
PL187218B1 (pl)	1995-06-07	2004-06-30	Danisco	Sposób wytwarzania polipeptydu, polipeptyd pochodzący z gatunku alg morskich, rekombinowana cząsteczka DNA, komórka drobnoustroju, sposób wytwarzaniaproduktu spożywczego, sposób wytwarzania paszy zwierzęcej, sposób redukowania zawartości cukru w produkcie spożywczym, sposób wytwarzania produktu, sposób wytwarzania produktu pieczonego z ciasta, kompozycja polepszająca ciasto, sposób analizowania zawartości cukru w próbce, sposób wytwarzania laktonu
PL184045B1 (pl) *	1995-06-07	2002-08-30	Danisco	Sposób polepszania reologicznych właściwości ciasta z mąki oraz jakości wytworzonego z ciasta wyrobu gotowego
WO1998044804A1 (en)	1997-04-09	1998-10-15	Danisco A/S	Improved method for preparing flour doughs and products made from such doughs using glycerol oxidase
ATE200848T1 (de)	1995-12-20	2001-05-15	Novozymes As	Verwendung von pyranose-oxidase beim backen
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
JP4417550B2 (ja)	1997-12-22	2010-02-17	ノボザイムスアクティーゼルスカブ	糖質酸化酵素およびベーキングにおけるその使用
EP1131416B1 (en)	1998-11-27	2009-09-02	Novozymes A/S	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
CA2392116A1 (en)	1999-12-03	2001-06-07	Danisco A/S	Method of improving dough and bread quality
WO2002000852A2 (en)	2000-06-26	2002-01-03	Novozymes A/S	Lipolytic enzyme
AU7235901A (en)	2000-07-06	2002-01-21	Novozymes As	Method of preparing a dough or a baked product made from a dough, with addition of lipolytic enzymes
DK1363506T3 (da)	2001-02-21	2006-03-20	Novozymes As	Fremstilling af stivelsesholdige födevareprodukter
EP1404827A2 (en)	2001-02-23	2004-04-07	Novozymes A/S	Lipolytic enzyme genes

1996
- 1996-06-04 PL PL96324689A patent/PL187218B1/pl unknown
- 1996-06-04 DE DE69623473T patent/DE69623473T3/de not_active Expired - Lifetime
- 1996-06-04 CN CNB961955767A patent/CN1266275C/zh not_active Expired - Lifetime
- 1996-06-04 NZ NZ310420A patent/NZ310420A/xx not_active IP Right Cessation
- 1996-06-04 EP EP96918616A patent/EP0832245B2/en not_active Expired - Lifetime
- 1996-06-04 DK DK96918616T patent/DK0832245T4/da active
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- 1996-06-04 JP JP50009097A patent/JP3917183B2/ja not_active Expired - Lifetime
- 1996-06-04 CO CO96028893A patent/CO4520252A1/es unknown
- 1996-06-04 AU AU61215/96A patent/AU705562B2/en not_active Expired
- 1996-06-04 AR AR10289596A patent/AR002301A1/es active IP Right Grant
- 1996-06-04 PH PH11996053280A patent/PH11996053280B1/en unknown
- 1996-06-04 AT AT96918616T patent/ATE223489T1/de active
- 1996-06-04 BR BRPI9609230A patent/BRPI9609230B1/pt not_active IP Right Cessation
- 1996-06-04 WO PCT/DK1996/000238 patent/WO1996040935A1/en active IP Right Grant
- 1996-06-04 US US08/669,304 patent/US6251626B1/en not_active Expired - Lifetime
- 1996-06-04 EP EP00101681A patent/EP1020523A3/en not_active Withdrawn
- 1996-06-04 ZA ZA964616A patent/ZA964616B/xx unknown
- 1996-06-04 ES ES96918616T patent/ES2182986T5/es not_active Expired - Lifetime
- 1996-06-04 CA CA002224143A patent/CA2224143C/en not_active Expired - Lifetime
- 1996-06-27 TW TW085107718A patent/TW438887B/zh not_active IP Right Cessation
1997
- 1997-12-05 NO NO19975693A patent/NO324271B1/no not_active IP Right Cessation
2001
- 2001-04-03 US US09/824,053 patent/US6924366B2/en not_active Expired - Fee Related
2004
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2005
- 2005-12-05 AR ARP050105062A patent/AR051696A2/es active IP Right Grant
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Also Published As

Publication number	Publication date
DK0832245T3 (da)	2003-01-06
EP1020523A2 (en)	2000-07-19
AU705562B2 (en)	1999-05-27
AR002301A1 (es)	1998-03-11
EP1020523A3 (en)	2000-08-30
ES2182986T3 (es)	2003-03-16
MY116524A (en)	2004-02-28
NO975693L (no)	1998-02-05
PH11996053280B1 (en)	2007-10-11
NZ310420A (en)	2000-01-28
JPH11511008A (ja)	1999-09-28
BR9609230A (pt)	1999-12-21
PL187218B1 (pl)	2004-06-30
AU6121596A (en)	1996-12-30
BRPI9609230B1 (pt)	2016-03-08
ATE223489T1 (de)	2002-09-15
CN1190992A (zh)	1998-08-19
CO4520252A1 (es)	1997-10-15
NO975693D0 (no)	1997-12-05
US7544795B2 (en)	2009-06-09
DK0832245T4 (da)	2009-01-26
ES2182986T5 (es)	2009-03-01
ZA964616B (en)	1996-12-12
CA2224143C (en)	2009-10-27
JP3917183B2 (ja)	2007-05-23
DE69623473T3 (de)	2009-04-23
TW438887B (en)	2001-06-07
CA2224143A1 (en)	1996-12-19
DE69623473T2 (de)	2003-04-30
US7727572B2 (en)	2010-06-01
EP0832245B2 (en)	2008-09-10
US20020106725A1 (en)	2002-08-08
CN1266275C (zh)	2006-07-26
EP0832245A1 (en)	1998-04-01
WO1996040935A1 (en)	1996-12-19
US6924366B2 (en)	2005-08-02
US20090041899A1 (en)	2009-02-12
PL324689A1 (en)	1998-06-08
AR051696A2 (es)	2007-01-31
DE69623473D1 (de)	2002-10-10
US6251626B1 (en)	2001-06-26
EP0832245B1 (en)	2002-09-04
US20050282249A1 (en)	2005-12-22
MX9709544A (es)	1998-10-31

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Publication	Publication Date	Title
NO324271B1 (no)	2007-09-17	Rekombinant heksoseoksidasepolypeptid (HOX), rekombinant DNA molekyl, fremgangsmate for fremstilling av HOX-polypeptidet og anvendelse av et slikt enzym i et naeringsprodukt.
US6358543B1 (en)	2002-03-19	Method of improving the properties of a flour dough, a flour dough improving composition and improved food products
US5879664A (en)	1999-03-09	Fungal protein disulfide isomerase
Lindgren et al.	1983	Silage fermentation of fish or fish waste products with lactic acid bacteria
CN1452656B (zh)	2011-06-15	脂肪氧合酶
US8178090B2 (en)	2012-05-15	Recombinant hexose oxidase
EP0565172A1 (en)	1993-10-13	Cloning and expression of DNA encoding a ripening form of a polypeptide having sulfhydryl oxidase activity
US8338153B2 (en)	2012-12-25	Recombinant hexose oxidase, a method of producing same and use of such enzyme
MXPA97009544A (es)	1999-01-11	Hexosa oxidasa recombinante, un metodo para producir la misma y el uso de tal enzima
EP1789541A2 (en)	2007-05-30	Overexpressed and purified aspergillus ficuum oxidase and nucleic acid encoding the same
WO2002061068A2 (en)	2002-08-08	Oxidase free of catalase side activities