FI105695B - Subtilisiinin analogeja, menetelmä niiden valmistamiseksi, niiden käyttö ja niitä koodaava DNA-sekvenssi - Google Patents

Subtilisiinin analogeja, menetelmä niiden valmistamiseksi, niiden käyttö ja niitä koodaava DNA-sekvenssi Download PDF

Info

Publication number: FI105695B
Authority: FI; Finland
Prior art keywords: subtilisin; asn; ser109; ser218; bacillus
Prior art date: 1987-04-10

Application number

FI885719A

Other languages

English (en)

Finnish (fi)

Swedish (sv)

Other versions

FI885719L (fi

FI885719A0 (fi

Inventor

Yitzhak Stabinsky

Mark M Zukowski

Michael Levitt

Original Assignee

Amgen Inc

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.)

1987-04-10

Filing date

1988-12-09

Publication date

2000-09-29

Family has litigation

First worldwide family litigation filed litigation Critical https://patents.darts-ip.com/?family=21891131&utm_source=google_patent&utm_medium=platform_link&utm_campaign=public_patent_search&patent=FI105695(B) "Global patent litigation dataset” by Darts-ip is licensed under a Creative Commons Attribution 4.0 International License.

1988-12-09 Application filed by Amgen Inc filed Critical Amgen Inc

1988-12-09 Publication of FI885719L publication Critical patent/FI885719L/fi

1988-12-09 Publication of FI885719A0 publication Critical patent/FI885719A0/fi

2000-09-29 Application granted granted Critical

2000-09-29 Publication of FI105695B publication Critical patent/FI105695B/fi

Links

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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
- C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
- 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)
- C12N9/48—Hydrolases (3) acting on peptide bonds (3.4)
- C12N9/50—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25)
- C12N9/52—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from bacteria or Archaea
- C12N9/54—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from bacteria or Archaea bacteria being Bacillus
- 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
- C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
- C12N15/09—Recombinant DNA-technology
- C12N15/63—Introduction of foreign genetic material using vectors; Vectors; Use of hosts therefor; Regulation of expression
- C12N15/74—Vectors or expression systems specially adapted for prokaryotic hosts other than E. coli, e.g. Lactobacillus, Micromonospora
- C12N15/75—Vectors or expression systems specially adapted for prokaryotic hosts other than E. coli, e.g. Lactobacillus, Micromonospora for Bacillus
- 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
- C12N5/00—Undifferentiated human, animal or plant cells, e.g. cell lines; Tissues; Cultivation or maintenance thereof; Culture media therefor
- 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

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Health & Medical Sciences (AREA)
Life Sciences & Earth Sciences (AREA)
Engineering & Computer Science (AREA)
Genetics & Genomics (AREA)
Chemical & Material Sciences (AREA)
Organic Chemistry (AREA)
Wood Science & Technology (AREA)
Zoology (AREA)
Bioinformatics & Cheminformatics (AREA)
Biotechnology (AREA)
General Engineering & Computer Science (AREA)
Biomedical Technology (AREA)
Microbiology (AREA)
Biochemistry (AREA)
General Health & Medical Sciences (AREA)
Molecular Biology (AREA)
Plant Pathology (AREA)
Physics & Mathematics (AREA)
Biophysics (AREA)
Medicinal Chemistry (AREA)
Chemical Kinetics & Catalysis (AREA)
General Chemical & Material Sciences (AREA)
Cell Biology (AREA)
Detergent Compositions (AREA)
Micro-Organisms Or Cultivation Processes Thereof (AREA)
Enzymes And Modification Thereof (AREA)
Preparation Of Compounds By Using Micro-Organisms (AREA)
Cosmetics (AREA)
Peptides Or Proteins (AREA)
Medicines Containing Material From Animals Or Micro-Organisms (AREA)

FI885719A 1987-04-10 1988-12-09 Subtilisiinin analogeja, menetelmä niiden valmistamiseksi, niiden käyttö ja niitä koodaava DNA-sekvenssi FI105695B (fi)

Applications Claiming Priority (4)

Application Number	Priority Date	Filing Date	Title
US3687287		1987-04-10
US07/036,872 US4914031A (en)	1987-04-10	1987-04-10	Subtilisin analogs
PCT/US1988/001038 WO1988008033A1 (fr)	1987-04-10	1988-03-28	Analogues de subtilisine
US8801038		1988-03-28

Publications (3)

Publication Number	Publication Date
FI885719L FI885719L (fi)	1988-12-09
FI885719A0 FI885719A0 (fi)	1988-12-09
FI105695B true FI105695B (fi)	2000-09-29

Family

ID=21891131

Family Applications (1)

Application Number	Title	Priority Date	Filing Date
FI885719A FI105695B (fi)	1987-04-10	1988-12-09	Subtilisiinin analogeja, menetelmä niiden valmistamiseksi, niiden käyttö ja niitä koodaava DNA-sekvenssi

Country Status (14)

Country	Link
US (1)	US4914031A (fr)
EP (1)	EP0309565B2 (fr)
JP (1)	JP2590247B2 (fr)
KR (1)	KR960006120B1 (fr)
AT (1)	ATE119941T1 (fr)
AU (1)	AU612653B2 (fr)
CA (1)	CA1316473C (fr)
DE (1)	DE3853328T3 (fr)
DK (1)	DK175576B1 (fr)
FI (1)	FI105695B (fr)
IL (1)	IL85953A (fr)
LV (1)	LV11043B (fr)
NO (1)	NO179679C (fr)
WO (1)	WO1988008033A1 (fr)

Families Citing this family (113)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
US5185258A (en) *	1984-05-29	1993-02-09	Genencor International, Inc.	Subtilisin mutants
WO1987004461A1 (fr) *	1986-01-15	1987-07-30	Amgen	ANALOGUES DE SUBTILISINE THERMIQUEMENT STABLE ET STABLE AU pH, ET LEUR PROCEDE DE PRODUCTION
DE3750916T2 (de) *	1986-04-30	1995-06-01	Genencor Int	Mutante einer nicht menschlichen Carbonyl-Hydrolase, für diese kodierende DNS-Sequenzen und Vektoren und durch diese Vektoren transformierte Wirte.
US5260207A (en) *	1987-04-06	1993-11-09	Enzon Labs Inc.	Engineering of electrostatic interactions at metal ion binding sites for the stabilization of proteins
WO1988008028A1 (fr) *	1987-04-06	1988-10-20	Genex Corporation	Stabilisation de proteines par mise au point des interactions electrostatiques aux sites de liaison d'ions metalliques
DK6488D0 (da) *	1988-01-07	1988-01-07	Novo Industri As	Enzymer
US6287841B1 (en)	1988-02-11	2001-09-11	Genencor International, Inc.	High alkaline serine protease
CN1056187C (zh) *	1988-02-11	2000-09-06	金克克国际有限公司	新的蛋白水解酶及其在洗涤剂中的应用
US5324653A (en) *	1988-02-11	1994-06-28	Gist-Brocades N.V.	Recombinant genetic means for the production of serine protease muteins
US5246849A (en) *	1988-04-12	1993-09-21	Enzon, Inc.	Thermally stable serine proteases
US5116741A (en) *	1988-04-12	1992-05-26	Genex Corporation	Biosynthetic uses of thermostable proteases
US5122449A (en) *	1988-10-07	1992-06-16	Eastman Kodak Company	Use of a protease in the extraction of chlamydial, gonococcal and herpes antigens
KR100188532B1 (ko) *	1989-05-17	1999-06-01	스티븐 엠. 오드리	돌연변이 섭티리신 및 그를 함유하는 조성물
ES2227508T3 (es) *	1989-06-26	2005-04-01	Unilever N.V.	Composiciones detergentes enzimaticas.
US5665587A (en) *	1989-06-26	1997-09-09	Novo Nordisk A/S	Modified subtilisins and detergent compositions containing same
DK316989D0 (da) *	1989-06-26	1989-06-26	Novo Nordisk As	Enzymer
US5658871A (en) *	1989-07-07	1997-08-19	Lever Brothers Company, Division Of Conopco, Inc.	Microbial lipase muteins and detergent compositions comprising same
ES2144990T3 (es) *	1989-08-25	2000-07-01	Henkel Of America Inc	Enzima proteolitica alcalina y metodo de produccion.
US6271012B1 (en) *	1989-10-11	2001-08-07	Genencor International, Inc.	Protease muteins and their use in detergents
US5541062A (en) *	1990-02-23	1996-07-30	Arch Development Corporation	Methods and compositions for preparing protein processing enzymes
IT1239733B (it) *	1990-02-23	1993-11-15	Eniricerche Spa	Mutanti della proteasi neutra termostabili e mezzi e metodi per la loro preparazione
DK271490D0 (da) *	1990-11-14	1990-11-14	Novo Nordisk As	Detergentkomposition
US5340735A (en)	1991-05-29	1994-08-23	Cognis, Inc.	Bacillus lentus alkaline protease variants with increased stability
EP0995801A1 (fr) *	1991-07-27	2000-04-26	Genencor International GmbH	Procédé d'amélioration de la stabilité d'enzymes et enzymes stabilisées
US5399484A (en) *	1991-10-08	1995-03-21	Eastman Kodak Company	Use of blocking protein with high pH extraction in method to determine a microorganism associated with periodontal disease and kit useful therefor
US5567601A (en) *	1993-06-01	1996-10-22	University Of Maryland	Subtilisin mutants lacking a primary calcium binding site
US5470733A (en) *	1993-06-01	1995-11-28	University Of Maryland	Calcium free subtilisin mutants
US6440717B1 (en)	1993-09-15	2002-08-27	The Procter & Gamble Company	BPN′ variants having decreased adsorption and increased hydrolysis
US6436690B1 (en) *	1993-09-15	2002-08-20	The Procter & Gamble Company	BPN′ variants having decreased adsorption and increased hydrolysis wherein one or more loop regions are substituted
DE69434962T2 (de) *	1993-10-14	2008-01-17	The Procter & Gamble Company, Cincinnati	Proteasehaltige reinigungsmittel
MA23346A1 (fr) *	1993-10-14	1995-04-01	Genencor Int	Variantes de la subtilisine
ES2199978T3 (es) *	1993-10-14	2004-03-01	THE PROCTER & GAMBLE COMPANY	Composiciones de blanqueo que comprenden enzimas proteasa.
CN1064074C (zh) *	1993-12-03	2001-04-04	巴科曼实验室国际公司	用嵌段共聚物促使酶稳定
US6599730B1 (en)	1994-05-02	2003-07-29	Procter & Gamble Company	Subtilisin 309 variants having decreased adsorption and increased hydrolysis
US6066611A (en) *	1994-10-13	2000-05-23	The Procter & Gamble Company	Bleaching compositions comprising protease enzymes
US6455295B1 (en)	1995-03-08	2002-09-24	The Procter & Gamble Company	Subtilisin Carlsberg variants having decreased adsorption and increased hydrolysis
US6475765B1 (en) *	1995-03-09	2002-11-05	Procter & Gamble Company	Subtilisin DY variants having decreased adsorption and increased hydrolysis
IL117350A0 (en)	1995-03-09	1996-07-23	Procter & Gamble	Proteinase k variants having decreased adsorption and increased hydrolysis
AU4772697A (en)	1996-11-04	1998-05-29	Novo Nordisk A/S	Subtilase variants and compositions
CN1530443A (zh)	1996-11-04	2004-09-22	ŵ��÷��޹�˾	枯草杆菌酶变异体和组合物
WO1999011768A1 (fr)	1997-08-29	1999-03-11	Novo Nordisk A/S	Variants de la protease et compositions
BR9811412A (pt)	1997-08-29	2000-08-22	Novo Nordisk As	Variante de enzima subtilase tendo melhorado desempenho de lavagem em detergentes, sequência de dna isolada, vetor de expressão, célula hospedeira microbiana, processos para produzir uma variante e para identificar uma variante de protease, composição, e, uso de uma variante de subtilase
ES2367505T3 (es) *	1997-10-23	2011-11-04	Danisco Us Inc.	Variantes de proteasa con sustituciones múltiples con carga neta alterada para usar en detergentes.
ATE298791T1 (de)	1997-11-21	2005-07-15	Novozymes As	Protease-varianten und zusammensetzungen
US6780629B2 (en)	1997-11-21	2004-08-24	Novozymes A/S	Subtilase enzymes
US6773907B2 (en)	1997-11-21	2004-08-10	Peter Kamp Hansen	Subtilase enzymes
US6908757B1 (en)	1998-03-26	2005-06-21	The Procter & Gamble Company	Serine protease variants having amino acid deletions and substitutions
US6495136B1 (en)	1998-03-26	2002-12-17	The Procter & Gamble Company	Proteases having modified amino acid sequences conjugated to addition moieties
BR9909130A (pt) *	1998-03-26	2000-12-19	Procter & Gamble	Variantes de protease de serina tendo substituições de amino-ácido
US6642011B2 (en)	1998-04-15	2003-11-04	Genencor International, Inc.	Human protease and use of such protease for pharmaceutical applications and for reducing the allergenicity of non-human proteins
US6376450B1 (en)	1998-10-23	2002-04-23	Chanchal Kumar Ghosh	Cleaning compositions containing multiply-substituted protease variants
US6831053B1 (en)	1998-10-23	2004-12-14	The Procter & Gamble Company	Bleaching compositions comprising multiply-substituted protease variants
ATE504651T1 (de)	1998-12-18	2011-04-15	Novozymes As	Subtilase enzyme der i-s1- und i-s2-untergruppen mit einem zusätzlichen aminosäurerest in einer aktiven schleifenregion
AU4392800A (en)	1999-05-20	2000-12-12	Novozymes A/S	Subtilase enzymes of the i-s1 and i-s2 sub-groups having at least one additionalamino acid residue between positions 126 and 127
EP1183337B1 (fr)	1999-05-20	2008-09-17	Novozymes A/S	Enzymes subtilases des sous-groupes i-s1 et i-s2 renfermant au moins un residu d'acide amine supplementaire entre les positions 132 et 133
WO2000071691A1 (fr)	1999-05-20	2000-11-30	Novozymes A/S	Enzymes de subtilase des sous-groupes i-s1 et i-s2 possedant au moins un residu supplementaire d'acide amine entre les positions 125 et 126
AU4392700A (en)	1999-05-20	2000-12-12	Novozymes A/S	Subtilase enzymes of the i-s1 and i-s2 sub-groups having at least one additionalamino acid residue between positions 129 and 130
EP1183341B2 (fr)	1999-05-20	2012-05-02	Novozymes A/S	Enzymes subtilases des sous groupes i-s1 et i-s2 possedant au moins un residu acide amine supplementaire entre les positions 127 et 128
WO2000071690A1 (fr)	1999-05-20	2000-11-30	Novozymes A/S	Enzymes subtilases des -sous groupes i-s1 et i-s2 possedant au moins un residu acide amine supplementaire entre les positions 128 et 129
KR20020021397A (ko) *	1999-07-22	2002-03-20	데이비드 엠 모이어	규정된 에피토프 영역에 아미노산 결실 및 치환을 갖는서브틸리신 프로테아제 변이체
US6946128B1 (en)	1999-07-22	2005-09-20	The Procter & Gamble Company	Protease conjugates having sterically protected epitope regions
CA2376045A1 (fr)	1999-07-22	2001-02-01	The Procter & Gamble Company	Proteases variantes de la subtilisine par substitutions acide amine dans des regions definies de l'epitope
BR0012694A (pt)	1999-07-22	2002-04-09	Procter & Gamble	Conjugado de protease, composição de limpeza e composição de tratamento pessoal
US6727085B2 (en) *	1999-12-15	2004-04-27	Fanoe Tina Sejersgaard	Subtilase variants having an improved wash performance on egg stains
US6777218B1 (en)	2000-03-14	2004-08-17	Novozymes A/S	Subtilase enzymes having an improved wash performance on egg stains
US7087415B2 (en) *	2000-07-31	2006-08-08	Athena Biotechnologies, Inc.	Methods and compositions for directed gene assembly
US6541234B1 (en) *	2000-09-11	2003-04-01	University Of Maryland Biotechnology Institute	Calcium free subtilisin mutants
US6541235B1 (en) *	2000-09-29	2003-04-01	University Of Maryland Biotechnology Institute	Calcium free subtilisin mutants
AU2002256624B2 (en)	2001-02-19	2007-12-06	Merck Patent Gmbh	Method for identification of T-cell epitopes and use for preparing molecules with reduced immunogenicity
PL210859B1 (pl) *	2001-03-23	2012-03-30	Genencor Int	Odmiana subtylizyny zawierająca zmieniony epitop limfocytów T, kwas nukleinowy kodujący tę odmianę subtylizyny, wektor ekspresyjny i komórka gospodarza zawierająca kwas nukleinowy oraz kompozycje zawierające tę odmianę subtylizyny
DE10153792A1 (de)	2001-10-31	2003-05-22	Henkel Kgaa	Neue Alkalische Protease-Varianten und Wasch- und Reinigungsmittel enthaltend diese neuen Alkalischen Protease-Varianten
DE10162728A1 (de)	2001-12-20	2003-07-10	Henkel Kgaa	Neue Alkalische Protease aus Bacillus gibsonii (DSM 14393) und Wasch-und Reinigungsmittel enthaltend diese neue Alkalische Protease
DE10162727A1 (de)	2001-12-20	2003-07-10	Henkel Kgaa	Neue Alkalische Protease aus Bacillus gibsonii (DSM 14391) und Wasch-und Reinigungsmittel enthaltend diese neue Alkalische Protease
DE10163884A1 (de)	2001-12-22	2003-07-10	Henkel Kgaa	Neue Alkalische Protease aus Bacillus sp. (DSM 14392) und Wasch- und Reinigungsmittel enthaltend diese neue Alkalische Protease
WO2003062380A2 (fr) *	2002-01-16	2003-07-31	Genencor International, Inc.	Variants de protease a substitutions multiples
EP1495128B1 (fr) *	2002-03-29	2014-05-07	Genencor International, Inc.	Expression proteinique amelioree dans bacillus
US7294499B2 (en) *	2003-01-30	2007-11-13	Novozymes A/S	Subtilases
CN102766545B (zh) *	2003-05-07	2014-08-06	诺维信公司	变体枯草杆菌蛋白酶（枯草杆菌酶）
WO2005040372A1 (fr)	2003-10-23	2005-05-06	Novozymes A/S	Protease a stabilite amelioree dans les detergents
DE10360805A1 (de)	2003-12-23	2005-07-28	Henkel Kgaa	Neue Alkalische Protease und Wasch- und Reinigungsmittel, enthaltend diese neue Alkalische Protease
EP2305821A3 (fr) *	2004-02-13	2011-04-13	Novozymes A/S	Variants de protéases
WO2006033668A2 (fr) *	2004-04-09	2006-03-30	Genencor International, Inc.	Modifications de pcka et expression amelioree de proteine chez un bacille
DE102004019751A1 (de)	2004-04-23	2005-11-17	Henkel Kgaa	Neue Alkalische Proteasen und Wasch- und Reinigungsmittel, enthaltend diese neuen Alkalischen Proteasen
KR100750659B1 (ko) *	2005-02-18	2007-08-20	인하대학교 산학협력단	계면활성제 및 산화제에 매우 안정한 호염, 호알카리성 단백질 분해효소 및 이를 암호화하는 유전자
US20100029538A1 (en)	2006-04-14	2010-02-04	Anna-Liisa Auterinen	One-Step Treatment of Textiles
JP2009534022A (ja)	2006-04-20	2009-09-24	ノボザイムスアクティーゼルスカブ	卵のシミに対する洗浄能力が向上したサビナーゼ変異体
US20080090745A1 (en) *	2006-10-13	2008-04-17	Fox Bryan P	Expression of Streptomyces subtilism inhibitor (SSI) proteins in Bacillus and Streptomyces sp.
WO2008112258A2 (fr) *	2007-03-12	2008-09-18	Danisco Us Inc.	Protéases modifiées
KR101522042B1 (ko)	2007-04-30	2015-05-20	다니스코 유에스 인크.	메탈로프로테아제 세제 제제를 안정화시키기 위한 단백질 가수분해물의 용도
US8343735B2 (en) *	2007-05-10	2013-01-01	Danisco Us Inc.	Modified secretion system to increase expression of polypeptides in bacteria
SG148934A1 (en)	2007-06-11	2009-01-29	Novozymes As	A process for combined biopolishing and bleach clean-up
DE102007032111B4 (de)	2007-07-09	2017-07-20	Henkel Ag & Co. Kgaa	Neue Proteasen und Wasch- und Reinigungsmittel enthaltend diese Proteasen
DE102007036756A1 (de)	2007-08-03	2009-02-05	Henkel Ag & Co. Kgaa	Neue Proteasen und Wasch- und Reinigungsmittel, enthaltend diese neuen Proteasen
DE102007051092A1 (de) *	2007-10-24	2009-04-30	Henkel Ag & Co. Kgaa	Subtilisin aus Becillus pumilus und Wasch- und Reinigungsmittel enthaltend dieses neue Subtilisin
JP5629584B2 (ja)	2007-12-21	2014-11-19	ダニスコ・ユーエス・インク	バチルス内での促進されたタンパク質生成
MX2010010310A (es) *	2008-03-28	2010-10-08	Danisco Us Inc	Metodo para amplificar un locus en una celula bacteriana.
WO2009149144A2 (fr) *	2008-06-06	2009-12-10	Danisco Us Inc.	Compositions et procédés comprenant des protéases microbiennes variantes
AR076941A1 (es)	2009-06-11	2011-07-20	Danisco Us Inc	Cepa de bacillus para una mayor produccion de proteina
WO2012022777A1 (fr)	2010-08-19	2012-02-23	Novozymes A/S	Procédé de criblage d'une sporulation induite
EP2782988A1 (fr) *	2011-11-25	2014-10-01	Novozymes A/S	Variants de subtilase et polynucléotides codants pour ceux-ci
WO2015102814A1 (fr)	2013-12-31	2015-07-09	Danisco Us Inc.	Expression améliorée de protéine
EP3739029A1 (fr)	2014-07-04	2020-11-18	Novozymes A/S	Variants de subtilase et polynucléotides codant pour ceux-ci
US10683528B2 (en)	2014-12-16	2020-06-16	Danisco Us Inc	Enhanced protein expression
US20170369537A1 (en)	2014-12-19	2017-12-28	Danisco Us Inc.	Enhanced protein expression
EP3585910B1 (fr)	2017-02-24	2024-03-20	Danisco US Inc.	Compositions et procédés pour une production de protéines accrue dans bacillus licheniformis
US11879127B2 (en)	2017-08-23	2024-01-23	Danisco Us Inc.	Methods and compositions for efficient genetic modifications of Bacillus licheniformis strains
US20210032639A1 (en)	2017-09-13	2021-02-04	Danisco Us Inc.	Modified 5'-untranslated region (utr) sequences for increased protein production in bacillus
EP3703661A1 (fr)	2017-11-02	2020-09-09	Danisco US Inc.	Compositions de matrices solides à point de congélation abaissé pour la granulation à l'état fondu d'enzymes
CN111670244B (zh)	2018-01-03	2023-08-01	丹尼斯科美国公司	突变的和遗传修饰的芽孢杆菌属细胞及其用于增加蛋白质产生的方法
WO2020099491A1 (fr)	2018-11-14	2020-05-22	Novozymes A/S	Composition de soin buccal comprenant un polypeptide ayant une activité dnase
JP7787077B2 (ja)	2020-01-15	2025-12-16	ダニスコ・ユーエス・インク	バチルス・リケニフォルミス（ｂａｃｉｌｌｕｓｌｉｃｈｅｎｉｆｏｒｍｉｓ）における強化したタンパク質産生のための組成物及び方法
US20230332124A1 (en)	2020-08-24	2023-10-19	Novozymes A/S	Oral care composition comprising a fructanase
WO2023023644A1 (fr)	2021-08-20	2023-02-23	Danisco Us Inc.	Polynucléotides codant pour de nouvelles nucléases, leurs compositions et leurs procédés d'élimination de l'adn lors de la préparations de protéines

Family Cites Families (11)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
GB1240058A (en) *	1968-04-12	1971-07-21	Procter & Gamble	Enzyme-containing detergent compositions
US3623957A (en) *	1970-01-21	1971-11-30	Baxter Laboratories Inc	Preparation of microbial alkaline protease by fermentation with bacillus subtilis, variety licheniformis
US4760025A (en) *	1984-05-29	1988-07-26	Genencor, Inc.	Modified enzymes and methods for making same
NZ208612A (en) *	1983-06-24	1991-09-25	Genentech Inc	Method of producing "procaryotic carbonyl hydrolases" containing predetermined, site specific mutations
JPS60160884A (ja) *	1984-02-01	1985-08-22	Showa Denko Kk	酵素安定化法
DE3685769T2 (de) *	1985-04-15	1993-01-21	Procter & Gamble	Fluessige reinigungsmittel mit einer oberflaechenaktiven verbindung, einem proteolytischen enzym und borsaeure.
WO1987005050A1 (fr) *	1986-02-12	1987-08-27	Genex Corporation	Procede de mutagenese et de criblage et produit obtenu
DE3750916T2 (de) *	1986-04-30	1995-06-01	Genencor Int	Mutante einer nicht menschlichen Carbonyl-Hydrolase, für diese kodierende DNS-Sequenzen und Vektoren und durch diese Vektoren transformierte Wirte.
JPH0657151B2 (ja) *	1986-05-15	1994-08-03	昭和電工株式会社	酵素の安定化法
HUT50877A (en) *	1987-02-27	1990-03-28	Gist Brocades Nv	Process for producing stable gene amplification in chromosomal dna of procaryote microorganisms
WO1988008028A1 (fr) *	1987-04-06	1988-10-20	Genex Corporation	Stabilisation de proteines par mise au point des interactions electrostatiques aux sites de liaison d'ions metalliques

1987
- 1987-04-10 US US07/036,872 patent/US4914031A/en not_active Expired - Lifetime
1988
- 1988-03-28 JP JP63503622A patent/JP2590247B2/ja not_active Expired - Lifetime
- 1988-03-28 EP EP88904041A patent/EP0309565B2/fr not_active Expired - Lifetime
- 1988-03-28 AT AT88904041T patent/ATE119941T1/de not_active IP Right Cessation
- 1988-03-28 KR KR1019880701638A patent/KR960006120B1/ko not_active Expired - Fee Related
- 1988-03-28 DE DE3853328T patent/DE3853328T3/de not_active Expired - Lifetime
- 1988-03-28 WO PCT/US1988/001038 patent/WO1988008033A1/fr not_active Ceased
- 1988-03-28 AU AU17016/88A patent/AU612653B2/en not_active Expired
- 1988-03-31 IL IL85953A patent/IL85953A/xx not_active IP Right Cessation
- 1988-03-31 CA CA000563171A patent/CA1316473C/fr not_active Expired - Lifetime
- 1988-12-09 FI FI885719A patent/FI105695B/fi not_active IP Right Cessation
- 1988-12-09 DK DK198806867A patent/DK175576B1/da not_active IP Right Cessation
- 1988-12-09 NO NO885484A patent/NO179679C/no not_active IP Right Cessation
1995
- 1995-06-21 LV LVP-95-188A patent/LV11043B/en unknown

Also Published As

Publication number	Publication date
ATE119941T1 (de)	1995-04-15
EP0309565A4 (fr)	1990-02-05
IL85953A (en)	1993-01-31
KR890700668A (ko)	1989-04-26
NO885484L (no)	1989-02-09
DE3853328T2 (de)	1995-07-27
AU612653B2 (en)	1991-07-18
FI885719L (fi)	1988-12-09
NO885484D0 (no)	1988-12-09
EP0309565A1 (fr)	1989-04-05
EP0309565B2 (fr)	2001-08-22
KR960006120B1 (ko)	1996-05-09
AU1701688A (en)	1988-11-04
EP0309565B1 (fr)	1995-03-15
DK686788D0 (da)	1988-12-09
US4914031A (en)	1990-04-03
CA1316473C (fr)	1993-04-20
DE3853328T3 (de)	2002-06-06
JP2590247B2 (ja)	1997-03-12
LV11043B (en)	1996-06-20
JPH01502957A (ja)	1989-10-12
NO179679C (no)	1996-11-27
DK175576B1 (da)	2004-12-13
LV11043A (lv)	1996-02-20
DE3853328D1 (de)	1995-04-20
WO1988008033A1 (fr)	1988-10-20
IL85953A0 (en)	1988-09-30
FI885719A0 (fi)	1988-12-09
HK1007168A1 (en)	1999-04-01
NO179679B (no)	1996-08-19
DK686788A (da)	1988-12-09

Legal Events

Date	Code	Title	Description
2004-08-31	FG	Patent granted	Owner name: AMGEN INC.
2008-04-22	MA	Patent expired

Publication	Publication Date	Title
CA1316473C (fr)	1993-04-20	Analogues de la subtilysine
CA2016211C (fr)	1998-07-21	Subtilisines ayant subi plusieurs mutations
FI102969B (fi)	1999-03-31	Lämpö- ja pH-stabiileja Bacillus-subtilisiinianalogeja, menetelmä niid en valmistamiseksi ja niitä sisältävä pesuainekoostumus
US5352604A (en)	1994-10-04	Alkaline proteolytic enzyme and method of production
EP0416967B1 (fr)	1994-12-28	Protéase alcaline
CA2023094C (fr)	2000-03-28	Production efficace de proteases de mutation
AU604476C (en)	1993-08-12	Thermally stable and pH stable subtilisin analogs and method for production thereof
HK1007168B (en)	1999-04-01	Subtilisins analogs
HK1006857B (en)	1999-03-19	Multiply mutated subtilisins
NO176844B (no)	1995-02-27	Enzymatisk aktive analoger av et Bacillus-subtilisin, nukleinsyre, vertscelle, fremgangsmåte for forbedring av varme- og pH-stabiliteten til et slikt subtilisin, samt vaskemiddelblanding som omfatter en slik analog