NO323106B1 - Konsensusprotein - Google Patents

Konsensusprotein Download PDF

Info

Publication number: NO323106B1
Authority: NO; Norway
Prior art keywords: phytase; amino acid; consensus; sequence; protein
Prior art date: 1997-07-24

Application number

NO19983364A

Other languages

English (en)

Norwegian (no)

Other versions

NO983364D0 (no

NO983364L (no

Inventor

Martin Lehmann

Original Assignee

Dsm Ip Assets Bv

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.)

1997-07-24

Filing date

1998-07-21

Publication date

2007-01-02

1998-07-21 Application filed by Dsm Ip Assets Bv filed Critical Dsm Ip Assets Bv

1998-07-21 Publication of NO983364D0 publication Critical patent/NO983364D0/no

1999-01-25 Publication of NO983364L publication Critical patent/NO983364L/no

2007-01-02 Publication of NO323106B1 publication Critical patent/NO323106B1/no

Links

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125000001493 tyrosinyl group Chemical group [H]OC1=C([H])C([H])=C(C([H])=C1[H])C([H])([H])C([H])(N([H])[H])C(*)=O 0.000 description 1
238000000108 ultra-filtration Methods 0.000 description 1
229940035893 uracil Drugs 0.000 description 1
238000002424 x-ray crystallography Methods 0.000 description 1
239000012138 yeast extract Substances 0.000 description 1
239000007222 ypd medium Substances 0.000 description 1

Classifications

- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K1/00—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/37—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from fungi
- C07K14/38—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from fungi from Aspergillus
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23K—FODDER
- A23K20/00—Accessory food factors for animal feeding-stuffs
- A23K20/10—Organic substances
- A23K20/142—Amino acids; Derivatives thereof
- A23K20/147—Polymeric derivatives, e.g. peptides or proteins
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23L—FOODS, FOODSTUFFS OR NON-ALCOHOLIC BEVERAGES, NOT OTHERWISE PROVIDED FOR; PREPARATION OR TREATMENT THEREOF
- A23L33/00—Modifying nutritive qualities of foods; Dietetic products; Preparation or treatment thereof
- A23L33/10—Modifying nutritive qualities of foods; Dietetic products; Preparation or treatment thereof using additives
- A23L33/17—Amino acids, peptides or proteins
- A23L33/18—Peptides; Protein hydrolysates
- 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)
- C12N9/16—Hydrolases (3) acting on ester bonds (3.1)
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides

Landscapes

Chemical & Material Sciences (AREA)
Life Sciences & Earth Sciences (AREA)
Health & Medical Sciences (AREA)
Organic Chemistry (AREA)
Genetics & Genomics (AREA)
Molecular Biology (AREA)
Engineering & Computer Science (AREA)
Proteomics, Peptides & Aminoacids (AREA)
Zoology (AREA)
Biochemistry (AREA)
General Health & Medical Sciences (AREA)
Medicinal Chemistry (AREA)
Bioinformatics & Cheminformatics (AREA)
Polymers & Plastics (AREA)
Wood Science & Technology (AREA)
Mycology (AREA)
Biophysics (AREA)
Biotechnology (AREA)
Food Science & Technology (AREA)
General Engineering & Computer Science (AREA)
Microbiology (AREA)
Biomedical Technology (AREA)
Gastroenterology & Hepatology (AREA)
Analytical Chemistry (AREA)
Animal Husbandry (AREA)
Nutrition Science (AREA)
Enzymes And Modification Thereof (AREA)
Micro-Organisms Or Cultivation Processes Thereof (AREA)
Fodder In General (AREA)
Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
Polymers With Sulfur, Phosphorus Or Metals In The Main Chain (AREA)
Preparation Of Compounds By Using Micro-Organisms (AREA)

NO19983364A 1997-07-24 1998-07-21 Konsensusprotein NO323106B1 (no)

Applications Claiming Priority (1)

Application Number	Priority Date	Filing Date	Title
EP97112688		1997-07-24

Publications (3)

Publication Number	Publication Date
NO983364D0 NO983364D0 (no)	1998-07-21
NO983364L NO983364L (no)	1999-01-25
NO323106B1 true NO323106B1 (no)	2007-01-02

Family

ID=8227106

Family Applications (1)

Application Number	Title	Priority Date	Filing Date
NO19983364A NO323106B1 (no)	1997-07-24	1998-07-21	Konsensusprotein

Country Status (13)

Country	Link
US (5)	US6153418A (de)
EP (2)	EP1403377A1 (de)
JP (1)	JP4177922B2 (de)
KR (1)	KR100562603B1 (de)
CN (2)	CN1163596C (de)
BR (1)	BR9802576B1 (de)
CA (1)	CA2238613C (de)
DE (1)	DE69826944T2 (de)
DK (1)	DK0897985T3 (de)
ES (1)	ES2230639T3 (de)
NO (1)	NO323106B1 (de)
NZ (1)	NZ330940A (de)
TW (1)	TW577921B (de)

Families Citing this family (104)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
US6699704B1 (en)	1994-04-25	2004-03-02	Roche Vitamins Inc.	Heat tolerant phytases
CA2231948C (en)	1997-03-25	2010-05-18	F. Hoffmann-La Roche Ag	Modified phytases
NZ330940A (en)	1997-07-24	2000-02-28	F	Production of consensus phytases from fungal origin using computer programmes
US7432097B2 (en)	1997-08-13	2008-10-07	Verenium Corporation	Phytases, nucleic acids encoding them and methods of making and using them
US6183740B1 (en)	1997-08-13	2001-02-06	Diversa Corporation	Recombinant bacterial phytases and uses thereof
US6855365B2 (en)	1997-08-13	2005-02-15	Diversa Corporation	Recombinant bacterial phytases and uses thereof
US7078035B2 (en)	1997-08-13	2006-07-18	Diversa Corporation	Phytases, nucleic acids encoding them and methods for making and using them
US6720014B1 (en)	1997-08-13	2004-04-13	Diversa Corporation	Phytase-containing foodstuffs and methods of making and using them
WO1999049022A1 (en) *	1998-03-23	1999-09-30	Novo Nordisk A/S	Phytase variants
US6514495B1 (en)	1998-03-23	2003-02-04	Novozymes A/S	Phytase varinats
AU753475C (en) *	1998-03-23	2003-04-17	Novozymes A/S	Thermostable phytases in feed preparation and plant expression
AU2003203147B2 (en)	1998-03-23	2008-05-29	Novozymes A/S	Phytase variants
US6451572B1 (en)	1998-06-25	2002-09-17	Cornell Research Foundation, Inc.	Overexpression of phytase genes in yeast systems
EP0969089A1 (de) *	1998-06-29	2000-01-05	F. Hoffmann-La Roche Ag	Phytase-zusammensetzung
US6610519B1 (en)	1998-10-02	2003-08-26	Novozymes A/S	Solid phytase composition stabilized with lactic acid provided by corn steep liquor
ATE338110T1 (de) *	1999-01-22	2006-09-15	Novozymes As	Verbesserte phytasen
US6720174B1 (en)	1999-01-28	2004-04-13	Novozymes A/S	Phytases
MXPA01009809A (es)	1999-03-31	2002-07-30	Cornell Res Foundation Inc	Fosfatasas con actividad de fitasa mejorada.
US6303766B1 (en)	1999-05-14	2001-10-16	Virginia Tech Intellectual Properties, Inc.	Soybean phytase and nucleic acid encoding the same
EP1640451A1 (de)	1999-10-01	2006-03-29	Novozymes A/S	Sprühgetrocknetes Enzymprodukt
DE60043640D1 (de)	1999-10-11	2010-02-25	Dsm Ip Assets Bv	Kontinuierliche Fermentation
US6841370B1 (en)	1999-11-18	2005-01-11	Cornell Research Foundation, Inc.	Site-directed mutagenesis of Escherichia coli phytase
US6855548B2 (en)	2000-02-08	2005-02-15	F. Hoffman-La Roche Ag	Use of acid-stable proteases in animal feed
US6960462B2 (en)	2000-02-08	2005-11-01	Dsm Ip Assets B.V	Use of acid-stable subtilisin proteases in animal feed
DE10126970A1 (de) *	2001-06-01	2002-12-05	Krueger Gmbh & Co Kg	Phytasehaltige Zusammensetzung
KR20040029122A (ko)	2001-08-27	2004-04-03	신젠타 파티서페이션즈 아게	자가-프로세싱 식물 및 식물 부분
EP1438417B1 (de) *	2001-10-26	2014-05-14	Danisco US Inc.	Phytaseenzyme, für phytaseenzyme codierende nukleinsäure, sowie sie enthaltende vektoren und wirtszellen
ES2597503T3 (es)	2001-10-31	2017-01-19	Huvepharma Eood	Alimento para animales que contiene fitasa y método
DK1325982T3 (da)	2001-12-27	2007-06-11	Georgia Pacific France	Gaufreret papirblad
MY139056A (en)	2001-12-28	2009-08-28	Ab Enzymes Gmbh	Microbially-expressed thermotolerant phytase for animal feed
TW200305430A (en)	2001-12-28	2003-11-01	Syngenta Participations Ag	Thermotolerant phytase for animal feed
US7238378B2 (en)	2002-02-08	2007-07-03	Novozymes A/S	Phytase variants
DE10233082A1 (de) *	2002-07-19	2004-03-04	Amaxa Gmbh	Fluoreszierendes Protein
DE10233047A1 (de) *	2002-07-19	2004-02-26	Amaxa Gmbh	Verfahren zur Herstellung eines künstlichen Polypeptids und nach diesem Verfahren hergestelltes künstliches Protein
US7309505B2 (en)	2002-09-13	2007-12-18	Cornell Research Foundation, Inc.	Using mutations to improve Aspergillus phytases
US20040063184A1 (en)	2002-09-26	2004-04-01	Novozymes North America, Inc.	Fermentation processes and compositions
ES2291883T3 (es)	2003-02-07	2008-03-01	Novozymes A/S	Proteasas.
US20040253696A1 (en)	2003-06-10	2004-12-16	Novozymes North America, Inc.	Fermentation processes and compositions
DE602004027376D1 (de)	2003-06-19	2010-07-08	Novozymes As	Proteasen
US20060236414A1 (en)	2003-06-19	2006-10-19	Novozymes A/S	Proteases and methods for producing them
EP2308966A1 (de)	2003-10-10	2011-04-13	Novozymes A/S	Proteasen
DE602005007182D1 (de) *	2004-01-30	2008-07-10	Basf Se	Stabilisierte phytase enthaltende granulate
CA2560613C (en)	2004-03-22	2015-11-24	Solvay Pharmaceuticals Gmbh	Oral pharmaceutical compositions of lipase-containing products, in particular of pancreatin, containing surfactants
EP2258839B1 (de)	2004-06-21	2015-06-03	Novozymes A/S	Proteasen
DE202005021810U1 (de)	2004-09-27	2010-04-22	Novozymes A/S	Körnchen mit einem Kern und einer Beschichtung
CN100546778C (zh) *	2005-02-03	2009-10-07	比克-维奥利克斯公司	具有会合的侧表面的剃刀手柄
US7658922B2 (en)	2005-06-24	2010-02-09	Ab Enzymes Gmbh	Monoclonal antibodies, hybridoma cell lines, methods and kits for detecting phytase
KR101555058B1 (ko)	2005-07-29	2015-09-22	애보트 래버러토리즈 게엠베하	살균된 판크레아틴 분말의 제조방법
US9198871B2 (en)	2005-08-15	2015-12-01	Abbott Products Gmbh	Delayed release pancreatin compositions
US11266607B2 (en)	2005-08-15	2022-03-08	AbbVie Pharmaceuticals GmbH	Process for the manufacture and use of pancreatin micropellet cores
US7919297B2 (en)	2006-02-21	2011-04-05	Cornell Research Foundation, Inc.	Mutants of Aspergillus niger PhyA phytase and Aspergillus fumigatus phytase
DK2365064T3 (en)	2006-04-04	2015-03-30	Novozymes As	Phytasevarianter
US10072256B2 (en)	2006-05-22	2018-09-11	Abbott Products Gmbh	Process for separating and determining the viral load in a pancreatin sample
BRPI0713389A2 (pt)	2006-06-21	2012-04-17	Novozymes North America, Inc. e Novozymes A/S	processo para desengomagem e lavagem combinadas de um tecido engomado, e, composição
BRPI0714241A2 (pt)	2006-07-13	2013-03-12	Dsm Ip Assets Bv	uso de uma amilase bacteriana, mÉtodos para preparar uma composiÇço, para aumentar o produÇço de leite de animais da subfamÍlia bovinae, para aumentar a espessura de gordura no dorso de animais da sbufamÍlia bovinae, para aumenantar o ganho de peso e/ou proporÇço de conversço de raÇço de animais da subfamÍlia bovinae, e para melhorar a digestibilidade aparente e/ou desaparecimento de mÁteria seca de gÊneros alimentÍcios em animais da subfamÍlia bovinae, e, uso de uma amilase bacteriana, mÉtodos para preparar uma composiÇço, para aumentar o produÇço de leite de animais da subfamÍlia bovinae, para aumentar a espessura de gordura no dorso de animais da subfamÍlia bovinae, para aumentar o ganho de peso e/ou proporÇço de conversço de raÇço de animais da subfamÍlia bovinae, e para melhorar a digestibilidade aparente e/ou desaparecimento de matÉria seca de gÊneros alimenticÍcios em animais da subfamÍlia bovinae, e, composiÇço
WO2008017066A2 (en)	2006-08-03	2008-02-07	Cornell Research Foundation, Inc.	Phytases with improved thermal stability
ES2576580T3 (es)	2006-08-07	2016-07-08	Novozymes A/S	Gránulos de enzima para pienso para animales
WO2008017659A1 (en)	2006-08-07	2008-02-14	Novozymes A/S	Enzyme granules for animal feed
JP5643083B2 (ja) *	2007-03-26	2014-12-17	ノボザイムスアクティーゼルスカブ	ハフニア・フィターゼ
ES2526646T3 (es)	2007-04-09	2015-01-14	Novozymes A/S	Tratamiento enzimático para el desengrasado de pieles y pellejos
US8192734B2 (en)	2007-07-09	2012-06-05	Cornell University	Compositions and methods for bone strengthening
EP2116136A1 (de) *	2008-05-08	2009-11-11	Nederlandse Organisatie voor toegepast- natuurwetenschappelijk onderzoek TNO	Neue Phytasen
US8401798B2 (en) *	2008-06-06	2013-03-19	Dna Twopointo, Inc.	Systems and methods for constructing frequency lookup tables for expression systems
US7561973B1 (en)	2008-07-31	2009-07-14	Dna Twopointo, Inc.	Methods for determining properties that affect an expression property value of polynucleotides in an expression system
US8126653B2 (en) *	2008-07-31	2012-02-28	Dna Twopointo, Inc.	Synthetic nucleic acids for expression of encoded proteins
US7561972B1 (en)	2008-06-06	2009-07-14	Dna Twopointo, Inc.	Synthetic nucleic acids for expression of encoded proteins
US20110097779A1 (en)	2008-06-23	2011-04-28	Chee-Leong Soong	Processes for Producing Fermentation Products
EP2933329B1 (de)	2008-09-26	2017-05-17	Novozymes A/S	Hafnia-phytasevarianten
DK2398893T3 (en)	2009-02-19	2015-03-23	Novozymes As	PROCESS FOR BREWING FOR USING fungal or Bacterial
US8529608B2 (en)	2009-04-28	2013-09-10	Osteomed Llc	Bone plate with a transfixation screw hole
WO2010135588A2 (en)	2009-05-21	2010-11-25	Verenium Corporation	Phytases, nucleic acids encoding them and methods for making and using them
WO2011000924A1 (en)	2009-07-03	2011-01-06	Abbott Products Gmbh	Spray-dried amylase, pharmaceutical preparations comprising the same and use
CN102753680B (zh)	2009-12-11	2015-05-13	诺维信公司	蛋白酶变体
ES2758795T3 (es)	2010-03-26	2020-05-06	Novozymes As	Variantes de fitasa termoestables
EP2552934B1 (de)	2010-03-30	2015-07-15	Novozymes A/S	Rückgewinnung von kristallmetaboliten
CN102984961A (zh)	2010-06-11	2013-03-20	诺维信公司	减少食物中生物胺的方法
WO2012025462A1 (en)	2010-08-26	2012-03-01	Dsm Ip Assets B.V.	Phytase in ready-to-drink soft drinks
EP2734633B1 (de)	2011-07-22	2019-05-01	Novozymes North America, Inc.	Verfahren zur vorbehandlung von cellulosematerial und verbesserung deren hydrolyse
AU2012338741B2 (en)	2011-11-17	2015-12-03	Novonesis Animal Biosolutions Ag	Use of acid stable proteases in animal feed, preferably to increase performance of cocci-vaccinated broiler chickens
US9951364B2 (en)	2013-09-11	2018-04-24	Novozymes A/S	Processes for producing fermentation products
EP2910640B1 (de)	2014-02-25	2018-12-05	Biopract GmbH	Verfahren zur Verbesserung der Substratzersetzung in landwirtschaftlichen Biogasanlagen
ES2810198T3 (es)	2014-06-27	2021-03-08	Dsm Ip Assets Bv	Método para mejorar el valor nutricional del pienso para animales
BR112017016718A2 (pt)	2015-02-10	2018-06-19	Dsm Ip Assets Bv	um método para melhorar a digestibilidade de ração e o desempenho de crescimento
AU2016217852B2 (en)	2015-02-12	2019-01-17	Dsm Ip Assets B.V.	A method for improving feed digestibility in bovine animals
CN108699570A (zh)	2015-12-22	2018-10-23	诺维信公司	从酒糟水提取油的工艺
BR112018016889A2 (pt)	2016-02-23	2019-02-12	Da Volterra	variantes de beta-lactamase
US10988749B2 (en)	2016-02-23	2021-04-27	Da Volterra	Beta-lactamase variants
US12227784B2 (en)	2017-09-15	2025-02-18	Novozymes A/S	Enzyme blends and processes for improving the nutritional quality of animal feed
BR112020007814A2 (pt)	2017-10-23	2020-10-20	Novozymes A/S	processos para reduzir e/ou prevenir um aumento nos níveis de ácido lático em um sistema de fermentação de biocombustível e para produção de um produto de fermentação a partir de um material contendo amido, e, uso de um polipeptídeo, ou uma composição enzimática
JP7223015B2 (ja)	2017-10-25	2023-02-15	ダ・ヴォルテッラ	β－ラクタマーゼ変異体
CA3098718A1 (en)	2018-05-31	2019-12-05	Novozymes A/S	Processes for enhancing yeast growth and productivity
MX2021003035A (es)	2018-09-17	2021-08-11	Dsm Ip Assets Bv	Composiciones de alimento animal y usos de las mismas.
WO2020115179A1 (en)	2018-12-05	2020-06-11	Novozymes A/S	Use of an enzyme granule
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
BR112022002203A2 (pt)	2019-08-05	2022-09-06	Novozymes As	Misturas de enzimas e processos para produção de um ingrediente alimentar com alto teor de proteína a partir de um subproduto de vinhaça completa
MX2022006438A (es)	2019-12-16	2022-06-22	Novozymes As	Procesos para obtener productos de fermentacion.
CN115605094A (zh)	2020-05-15	2023-01-13	帝斯曼知识产权资产管理有限公司（Nl）	用于改善动物饲料的营养价值的方法
CA3189083A1 (en)	2020-08-13	2022-02-17	Novozymes A/S	Phytase variants and polynucleotides encoding same
EP4294426A1 (de)	2021-02-16	2023-12-27	DSM IP Assets B.V.	Verfahren zur reduzierung pathogener e. coli durch selektiven futterzusatzeingriff mit enzymen wie etwa muramidase
WO2022175263A2 (en)	2021-02-16	2022-08-25	Dsm Ip Assets B.V.	Methods of selectively promoting animal welfare through modulation of microbiome
KR20230150828A (ko)	2021-02-26	2023-10-31	디에스엠 아이피 어셋츠 비.브이.	세린 프로테아제를 사용함으로써 동물 사료에서 카보하이드라제에 의한 탄수화물 소화율을 향상시키는 방법
CN118434292A (zh)	2021-12-23	2024-08-02	诺维信专利公司	用于减少动物的氨气排放量的方法
WO2024047009A1 (en)	2022-08-30	2024-03-07	Dsm Ip Assets B.V.	Methods and uses for modifying gut flora in aquatic species
WO2025176789A1 (en)	2024-02-23	2025-08-28	Dsm Ip Assets B.V.	A method for reducing ammonia emission of aquatic animals

Family Cites Families (22)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
DE1492060C3 (de)	1965-09-08	1974-02-21	Nordmark-Werke Gmbh, 2000 Hamburg	Verfahren zur Stabilisierung wäßriger Pepsinlösungen
EP0035204B2 (de)	1980-03-05	1991-05-22	Miles Inc.	Pasteurisierte therapeutisch aktive Proteinzusammensetzungen
US6936694B1 (en) *	1982-05-06	2005-08-30	Intermune, Inc.	Manufacture and expression of large structural genes
US5780292A (en) *	1987-04-29	1998-07-14	Alko Group Ltd.	Production of phytate degrading enzymes in trichoderma
ES2056799T3 (es) *	1987-07-17	1994-10-16	Rhein Biotech Ges Fur Biotechn	Moleculas de adn codante para las regiones de control fmdh y gen estructural para una proteina que tiene una actividad de fmdh y su uso.
CZ289014B6 (cs) *	1989-09-27	2001-10-17	Dsm N. V.	Vyčiątěná a izolovaná sekvence DNA kódující fungální fytázu, konstrukt pro expresi, vektory a transformované hostitelské buňky a způsob produkce fytázy
UA27702C2 (uk) *	1989-09-27	2000-10-16	Гіст-Брокейдс Н.В.	Фрагмент геномної днк, що кодує фітазу aspergillus niger,фрагмент кднк, що кодує фітазу aspergillus niger, рекомбінантна плазмідна днк для експресії фітази в aspergillus (варіанти), штам aspergillus-продуцент фітази aspergillus (варіанти), спосіб одержання фітази, рекомбінанта фітаза aspergillus niger
GB9006642D0 (en)	1990-03-24	1990-05-23	Gibson Timothy D	Enzyme stabilisation
EP0626010A1 (de) *	1992-02-13	1994-11-30	Gist-Brocades N.V.	Stabilisierte, wässrige, flüssige, phytase enthaltende formulierungen
JPH09505201A (ja) *	1992-07-31	1997-05-27	パンラブスインコーポレイテッド	組換え細胞、ｄｎａ構造、ベクター及びフィチン酸塩分解酵素を任意の比率で発現する方法
DE69333071T2 (de) *	1993-04-05	2004-05-06	Aveve N.V.	Phytate-Hydrolyse und enzymatische Zusammensetzung für die Hydrolyse von Phytat
EP0705348B1 (de)	1993-06-21	2001-08-08	Roche Diagnostics Corporation	Stabilisator für diagnostische reagentien
US6291221B1 (en)	1994-04-25	2001-09-18	Roche Vitamins Inc.	Heat tolerant phytases
ES2268687T3 (es) *	1994-04-25	2007-03-16	Dsm Ip Assets B.V.	Polipeptidos con actividad fitasa.
US6358722B1 (en)	1994-04-25	2002-03-19	Roche Vitamins, Inc.	Heat tolerant phytases
US5853973A (en) *	1995-04-20	1998-12-29	American Cyanamid Company	Structure based designed herbicide resistant products
DE69631924T2 (de) *	1995-06-09	2004-08-12	Dsm Ip Assets B.V.	Fermentative Herstellung von Carotenoiden
CZ87497A3 (cs)	1995-07-28	1998-03-18	Gist-Brocades B. V.	Enzymové přípravky stabilizované pomocí solí
JP3143050B2 (ja)	1995-08-31	2001-03-07	オリエンタル酵母工業株式会社	安定化されたグルコース６リン酸脱水素酵素
CA2231948C (en) *	1997-03-25	2010-05-18	F. Hoffmann-La Roche Ag	Modified phytases
NZ501409A (en)	1997-06-04	2002-02-01	Dsm N	High-activity phytase compositions containing a carbohydrate polymer
NZ330940A (en)	1997-07-24	2000-02-28	F	Production of consensus phytases from fungal origin using computer programmes

1998
- 1998-07-10 NZ NZ330940A patent/NZ330940A/en unknown
- 1998-07-14 TW TW087111377A patent/TW577921B/zh not_active IP Right Cessation
- 1998-07-15 EP EP20030024497 patent/EP1403377A1/de not_active Withdrawn
- 1998-07-15 DE DE69826944T patent/DE69826944T2/de not_active Expired - Lifetime
- 1998-07-15 DK DK98113176T patent/DK0897985T3/da active
- 1998-07-15 EP EP98113176A patent/EP0897985B1/de not_active Expired - Lifetime
- 1998-07-15 ES ES98113176T patent/ES2230639T3/es not_active Expired - Lifetime
- 1998-07-21 CA CA2238613A patent/CA2238613C/en not_active Expired - Lifetime
- 1998-07-21 NO NO19983364A patent/NO323106B1/no not_active IP Right Cessation
- 1998-07-23 CN CNB981179495A patent/CN1163596C/zh not_active Expired - Lifetime
- 1998-07-23 US US09/121,425 patent/US6153418A/en not_active Expired - Lifetime
- 1998-07-23 CN CNA2004100043732A patent/CN1526815A/zh active Pending
- 1998-07-23 KR KR1019980029633A patent/KR100562603B1/ko not_active Expired - Lifetime
- 1998-07-24 BR BRPI9802576-7A patent/BR9802576B1/pt not_active IP Right Cessation
- 1998-07-24 JP JP20906398A patent/JP4177922B2/ja not_active Expired - Lifetime
2000
- 2000-08-08 US US09/634,493 patent/US6579975B1/en not_active Ceased
2003
- 2003-04-23 US US10/421,112 patent/US7052869B2/en not_active Expired - Lifetime
2005
- 2005-05-24 US US11/137,849 patent/USRE39649E1/en not_active Expired - Lifetime
2006
- 2006-03-28 US US11/392,781 patent/US20060172390A1/en not_active Abandoned

Also Published As

Publication number	Publication date
CA2238613A1 (en)	1999-01-24
CN1208768A (zh)	1999-02-24
US6153418A (en)	2000-11-28
KR19990014095A (ko)	1999-02-25
EP0897985A3 (de)	1999-12-22
JP4177922B2 (ja)	2008-11-05
NO983364D0 (no)	1998-07-21
ES2230639T3 (es)	2005-05-01
EP0897985A2 (de)	1999-02-24
JPH11146791A (ja)	1999-06-02
CN1163596C (zh)	2004-08-25
US6579975B1 (en)	2003-06-17
BR9802576B1 (pt)	2011-04-19
DK0897985T3 (da)	2005-01-17
DE69826944T2 (de)	2005-03-10
TW577921B (en)	2004-03-01
USRE39649E1 (en)	2007-05-22
EP0897985B1 (de)	2004-10-13
DE69826944D1 (de)	2004-11-18
US20060172390A1 (en)	2006-08-03
BR9802576A (pt)	2001-03-20
NO983364L (no)	1999-01-25
NZ330940A (en)	2000-02-28
US20030190677A1 (en)	2003-10-09
EP1403377A1 (de)	2004-03-31
CA2238613C (en)	2010-05-25
KR100562603B1 (ko)	2006-05-25
US7052869B2 (en)	2006-05-30
CN1526815A (zh)	2004-09-08

Legal Events

Date	Code	Title	Description
2011-02-28	MM1K	Lapsed by not paying the annual fees

Publication	Publication Date	Title
NO323106B1 (no)	2007-01-02	Konsensusprotein
US6391605B1 (en)	2002-05-21	Modified phytases
AU781520B2 (en)	2005-05-26	Improved phytases
CA2319658C (en)	2010-06-15	Continuous fermentation process
Van Hartingsveldt et al.	1993	Cloning, characterization and overexpression of the phytase-encoding gene (phyA) of Aspergillus niger
JPH09500014A (ja)	1997-01-07	菌類のタンパク質ジスルフィドイソメラーゼ
AU760737B2 (en)	2003-05-22	Phytase formulation
Svendsen et al.	1998	The amino acid sequences of carboxypeptidases I and II from Aspergillus niger and their stability in the presence of divalent cations