[go: up one dir, main page]

ES2498823T3 - Variante de lipasa - Google Patents

Variante de lipasa Download PDF

Info

Publication number
ES2498823T3
ES2498823T3 ES10180769.1T ES10180769T ES2498823T3 ES 2498823 T3 ES2498823 T3 ES 2498823T3 ES 10180769 T ES10180769 T ES 10180769T ES 2498823 T3 ES2498823 T3 ES 2498823T3
Authority
ES
Spain
Prior art keywords
wild type
amino acid
type lipase
lipase
negative
Prior art date
Legal status (The legal status 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 status listed.)
Expired - Lifetime
Application number
ES10180769.1T
Other languages
English (en)
Inventor
Jesper Vind
Allan Svendsen
Shamkant Anant Patkar
Kim V Andersen
Dorte A Halkier
Kirsten Bojsen
Current Assignee (The listed assignees may be inaccurate. Google has not performed a legal analysis and makes no representation or warranty as to the accuracy of the list.)
Novozymes AS
Original Assignee
Novozymes AS
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.)
Filing date
Publication date
Application filed by Novozymes AS filed Critical Novozymes AS
Application granted granted Critical
Publication of ES2498823T3 publication Critical patent/ES2498823T3/es
Anticipated expiration legal-status Critical
Expired - Lifetime legal-status Critical Current

Links

Classifications

    • C—CHEMISTRY; METALLURGY
    • C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
    • C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
    • C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
    • C11D3/16—Organic compounds
    • C11D3/38—Products with no well-defined composition, e.g. natural products
    • C11D3/386—Preparations containing enzymes, e.g. protease or amylase
    • C11D3/38627—Preparations containing enzymes, e.g. protease or amylase containing lipase
    • 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)
    • C12N9/18—Carboxylic ester hydrolases (3.1.1)
    • C12N9/20—Triglyceride splitting, e.g. by means of lipase

Landscapes

  • Chemical & Material Sciences (AREA)
  • Life Sciences & Earth Sciences (AREA)
  • Organic Chemistry (AREA)
  • Engineering & Computer Science (AREA)
  • Health & Medical Sciences (AREA)
  • Wood Science & Technology (AREA)
  • Bioinformatics & Cheminformatics (AREA)
  • Genetics & Genomics (AREA)
  • Zoology (AREA)
  • Chemical Kinetics & Catalysis (AREA)
  • Oil, Petroleum & Natural Gas (AREA)
  • Biomedical Technology (AREA)
  • Biotechnology (AREA)
  • Molecular Biology (AREA)
  • Microbiology (AREA)
  • Medicinal Chemistry (AREA)
  • Biochemistry (AREA)
  • General Engineering & Computer Science (AREA)
  • General Health & Medical Sciences (AREA)
  • Detergent Compositions (AREA)
  • Enzymes And Modification Thereof (AREA)
  • Micro-Organisms Or Cultivation Processes Thereof (AREA)

Abstract

Lipasa que es un polipéptido con una secuencia de aminoácidos que: a) tiene al menos un 90 % de identidad con la lipasa tipo salvaje derivada de la cepa de Humicola lanuginosa DSM 4109; b) en comparación con dicha lipasa tipo salvaje, comprende una sustitución de T231R; y i) comprende un aminoácido negativo en la posición E210 de dicha lipasa tipo salvaje; ii) comprende un aminoácido cargado negativamente en la región correspondiente a las posiciones 90-101 de dicha lipasa de tipo salvaje; y iii) comprende un aminoácido neutro o negativo en una posición correspondiente a N94 de dicha lipasa tipo salvaje y/o tiene una carga eléctrica neta neutra o negativa en la región correspondiente a las posiciones 90-101 de dicha lipasa tipo salvaje

Description

imagen1
imagen2
comprender la sustitución G91A.
[0026] La lipasa puede opcionalmente comprender sustituciones de uno o más aminoácidos adicionales. Tales sustituciones pueden, por ejemplo, ser hechas según principios conocidos en la técnica, por ejemplo sustituciones 5 descritas en WO92/05249, WO94/25577, WO95/22615, WO97/04079 y WO97/07202.
Combinaciones de sustituciones
[0027] Una variante de lipasa con buen rendimiento de primer lavado se puede obtener modificando la Lipolasa de la 10 siguiente manera. Las sustituciones entre paréntesis son opcionales.
T231R+ N233R
N94K+ D96L+ T231R+ N233R+ Q249R+ 270P+ 271G+ 272L
D96L+ T231R+ N233R
G91A+ E99K+ T231R+ N233R +Q249R
(N33Q) +D96L +T231R +N233R +Q249R +270PGL
R209P +T231R +N233R
(N33Q) +E99N +N101S +T231R +N233R +Q249R +270 PGL
K24C +(N33Q) +D96S +T231R +N233R +Q249R +270 PCL
(N33Q) +G91A +E99K +T231R +N233R +Q249R +270 PGL
E1A +(N33Q) +G91A +E99K +T231R +N233R +Q249R +270 PGL
(N33Q) +G91A +E99K +G255R +T231R +N233R +Q249R +270 PGL
(N33Q) +G91A +E99K +T231R +N233R +T244R +Q249R +270 PGL
G91A +E99K +T231R +N233R +Q249R
E87K +G91D +D96L +G225P +T231 R +N233R +Q249R +N251D
G91A +E99K +T231R +N233R +Q249R +270AGVF
G91A +E99K +T189G +T231R +N233R +Q249R
D102G +T231R +N233R +Q249R
T231R +N233R +Q249R +270AGVF
R209P +T231 R +N233R
N33Q +N94K +D96L +T231R +N233R +Q249R +270PGLPFKRV
N33Q +N94K +D96L +T231R +N233R +Q249R
N33Q +D96S +T231R +N233R +Q249R
N33Q +D96S +V2281 + +T231R +N233R +Q249R
E1A +N33Q +G91A +E99K +T231R +N233R +Q249R +270PGLPFKRV
N33Q +S83T +E87K +G91A + E99K +T231R +N233R +Q249R +270PGLPFKRV
N33Q +G91A + E99K +T231R +N233R +Q249R +270PGLPFKRV
T231R +N233R +270CP
T231R +N233R +270RE
N33Q +E99N +N101S +T231R +N233R +Q249R +270PGLPFKRV
D62A +S83T + G91A +E99K +T231R +N233R +Q249R
E99N +N101S +T231R +N233R +Q249R
R84W +G91A +E99K +T231 R +N233R +Q249R
G91A +E99K +T231R +N233R +Q249R +270SPG
G91A +E99K +T231R +N233R +Q249R +270VVVP
G91A +E99K +T231R +N233R +Q249R +270LLASSGRGGHR
G91A +E99K +T231R +N233R +Q249R +270VTT
G91A +E99K +T231R +N233R +Q249R +270VLQ
G91A +E99K +T231R +N233R +Q249R +270TST
G91A +E99K +T231R +N233R +Q249R +270LRI
V60G +D62E +G91A +E99K +T231R +N233R +Q249R
G91A +D96W +E99K +T231R +N233R +G263Q +L264A +I265T +G266S +T267A +L269N +270AGGFS
Nomenclatura para modificaciones de aminoácidos
15 [0028] La nomenclatura usada aquí para definir mutaciones es esencialmente como se describe en WO92/05249. Así, T231R indica una sustitución de T en la posición 231 con R. PGL o 270P+271 G+272L indica la adición peptídica PGL fijada al C-terminal (L269).
Agrupación de aminoácidos
20 [0029] En esta especificación, los aminoácidos se clasifican como cargados negativamente, cargados positivamente o eléctricamente neutros según su carga eléctrica a pH 10, que es típico del detergente de la invención. Así, los aminoácidos negativos son E, D, C (cisteína) e Y, particularmente E y D. Los aminoácidos positivos son R, K y H,
4
imagen3
imagen4
imagen5

Claims (1)

  1. imagen1
    imagen2
ES10180769.1T 1999-03-31 2000-03-30 Variante de lipasa Expired - Lifetime ES2498823T3 (es)

Applications Claiming Priority (2)

Application Number Priority Date Filing Date Title
DKPA199900441 1999-03-31
DK44199 1999-03-31

Publications (1)

Publication Number Publication Date
ES2498823T3 true ES2498823T3 (es) 2014-09-25

Family

ID=8093585

Family Applications (2)

Application Number Title Priority Date Filing Date
ES03024829.8T Expired - Lifetime ES2445330T3 (es) 1999-03-31 2000-03-30 Variante de lipasa
ES10180769.1T Expired - Lifetime ES2498823T3 (es) 1999-03-31 2000-03-30 Variante de lipasa

Family Applications Before (1)

Application Number Title Priority Date Filing Date
ES03024829.8T Expired - Lifetime ES2445330T3 (es) 1999-03-31 2000-03-30 Variante de lipasa

Country Status (6)

Country Link
EP (3) EP2277999B1 (es)
CN (1) CN100455663C (es)
BR (1) BRPI0009396B1 (es)
CA (1) CA2366843A1 (es)
DK (2) DK2277999T3 (es)
ES (2) ES2445330T3 (es)

Families Citing this family (13)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO2006084470A2 (en) * 2005-02-10 2006-08-17 Novozymes A/S Enzymatic enantioselective ester or amide hydrolysis or synthesis
CA2612648A1 (en) * 2005-06-24 2006-12-28 Novozymes A/S Lipases for pharmaceutical use
EP2371948B1 (en) * 2006-01-23 2017-04-19 Novozymes A/S Lipase variants
EP2455460A3 (en) 2006-12-21 2012-12-26 Novozymes A/S Lipase variants for pharmaceutical use
AU2013200626B2 (en) * 2006-12-21 2015-03-05 Novozymes A/S Lipase variants for pharmaceutical use
BRPI0909707A2 (pt) * 2008-02-29 2015-08-25 Procter & Gamble Composição detergente que compreende lipase.
WO2011072117A1 (en) 2009-12-09 2011-06-16 The Procter & Gamble Company Fabric and home care products
ES2887576T3 (es) * 2011-12-29 2021-12-23 Novozymes As Composiciones detergentes con variantes de lipasa
WO2013113622A1 (en) * 2012-02-03 2013-08-08 Novozymes A/S Lipase variants and polynucleotides encoding same
CA2887898A1 (en) * 2012-10-12 2014-04-17 Danisco Us Inc. Compositions and methods comprising a lipolytic enzyme variant
CN113862238A (zh) * 2014-12-22 2021-12-31 诺维信公司 洗涤剂组合物、脂肪酶变体以及编码其的多核苷酸
CN114292829A (zh) * 2015-07-06 2022-04-08 诺维信公司 脂肪酶变体以及编码它们的多核苷酸
BR112019023695A2 (pt) * 2017-05-12 2020-06-09 Basf Se formulação detergente, e, método de limpeza

Family Cites Families (16)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US4810414A (en) 1986-08-29 1989-03-07 Novo Industri A/S Enzymatic detergent additive
EP0305216B1 (en) 1987-08-28 1995-08-02 Novo Nordisk A/S Recombinant Humicola lipase and process for the production of recombinant humicola lipases
BR9106839A (pt) 1990-09-13 1993-07-20 Novo Nordisk As Variante de lipase,construcao de dna,vetor de expressao de recombinante,celula,planta,processo para produzir uma variante de lipase,aditivo e composicao de detergente
US5869438A (en) * 1990-09-13 1999-02-09 Novo Nordisk A/S Lipase variants
DK46693D0 (es) 1993-04-23 1993-04-23 Novo Nordisk As
JP3715328B2 (ja) * 1992-09-21 2005-11-09 株式会社東芝 データ処理装置
WO1995022615A1 (en) * 1994-02-22 1995-08-24 Novo Nordisk A/S A method of preparing a variant of a lipolytic enzyme
WO1996016154A1 (en) * 1994-11-18 1996-05-30 The Procter & Gamble Company Detergent compositions containing lipase and protease
DE69633825T2 (de) 1995-07-14 2005-11-10 Novozymes A/S Modifiziertes enzym mit lipolytischer aktivität
EP0851913B1 (en) * 1995-08-11 2004-05-19 Novozymes A/S Novel lipolytic enzymes
AU2382397A (en) 1996-04-25 1997-11-19 Novo Nordisk A/S Alkaline lipolytic enzyme
WO1997043375A1 (en) 1996-05-15 1997-11-20 The Procter & Gamble Company Detergent compositions comprising specific lipolytic enzyme and a specific surfactant system
EP0954569A1 (en) 1996-08-27 1999-11-10 Novo Nordisk A/S Novel lipolytic enzymes
AU3247699A (en) * 1998-02-17 1999-09-06 Novo Nordisk A/S Lipase variant
DK1131416T3 (da) * 1998-11-27 2009-10-26 Novozymes As Lipolytiske enzymvarianter
WO2003060112A1 (en) * 2002-01-16 2003-07-24 Novozymes A/S Lipolytic enzyme variants and method for their production

Also Published As

Publication number Publication date
CN1409760A (zh) 2003-04-09
DK2277999T3 (da) 2014-09-22
EP1428874A3 (en) 2004-07-14
EP1428874A2 (en) 2004-06-16
EP2277999B1 (en) 2014-07-02
BR0009396A (pt) 2002-01-08
EP2278000A1 (en) 2011-01-26
DK1428874T3 (en) 2014-03-10
CA2366843A1 (en) 2000-10-12
EP1428874B1 (en) 2013-12-18
EP2277999A1 (en) 2011-01-26
ES2445330T3 (es) 2014-03-03
CN100455663C (zh) 2009-01-28
BRPI0009396B1 (pt) 2021-01-05

Similar Documents

Publication Publication Date Title
ES2498823T3 (es) Variante de lipasa
Foltmann et al. The complete amino acid sequence of prochymosin.
Hong et al. A unified nomenclature for Arabidopsis dynamin-related large GTPases based on homology and possible functions
Peters Proteasomes: protein degradation machines of the cell
Kohama et al. Isolation of angiotensin-converting enzyme inhibitor from tuna muscle
Ugai et al. Purification and characterization of the 26S proteasome complex catalyzing ATP-dependent breakdown of ubiquitin-ligated prot from rat liver
Valente et al. Bothrops insularis venomics: a proteomic analysis supported by transcriptomic-generated sequence data
RU2009128067A (ru) Варианты липаз для их применения в фармацевтике
US20090029440A1 (en) Lipase Variants
Madeddu et al. Characterization of centrin genes in Paramecium
Lee et al. A unified view of low complexity regions (LCRs) across species
Futai et al. Molecular cloning of PalBH, a mammalian homologue of the Aspergillus atypical calpain PalB
DE60023860D1 (de) Verfahren zur herstellung von rekombinanten peptiden
Baumann et al. Planktocyclin, a cyclooctapeptide protease inhibitor produced by the freshwater cyanobacterium Planktothrix rubescens
ATE294856T1 (de) Lunasin peptide
Wang et al. Affinity purification and characterization of a cutinase from the fungal plant pathogen Monilinia fructicola (Wint.) honey
Lund et al. The human chromosomal protein HMG I contains two identical palindrome amino acid sequences
Munawar et al. Isolation and characterization of Bradykinin potentiating peptides from Agkistrodon bilineatus venom
Dohmae et al. The complete amino acid sequences of two serine proteinase inhibitors from the fruiting bodies of a basidiomycete, Pleurotus ostreatus
Wiens et al. Isolation of the silicatein-α interactor silintaphin-2 by a novel solid-phase pull-down assay
Park et al. High-level expression of the angiotensin-converting-enzyme-inhibiting peptide, YG-1, as tandem multimers in Escherichia coli
CA2296813A1 (en) Novel synthetic genes for plant gums
CN105622763A (zh) 抗菌肽融合蛋白及其制备方法和应用
Munawar et al. Venom peptide analysis of Vipera ammodytes meridionalis (Viperinae) and Bothrops jararacussu (Crotalinae) demonstrates subfamily-specificity of the peptidome in the family Viperidae
Lu et al. Characterization and cloning of a novel phospholipase A2 from the venom of Trimeresurus jerdonii snake