[go: up one dir, main page]

CA2373135A1 - Nouvelle xylanase alcalinophile thermostable - Google Patents

Nouvelle xylanase alcalinophile thermostable Download PDF

Info

Publication number
CA2373135A1
CA2373135A1 CA002373135A CA2373135A CA2373135A1 CA 2373135 A1 CA2373135 A1 CA 2373135A1 CA 002373135 A CA002373135 A CA 002373135A CA 2373135 A CA2373135 A CA 2373135A CA 2373135 A1 CA2373135 A1 CA 2373135A1
Authority
CA
Canada
Prior art keywords
protein
sequence
amino acid
xylanase
sequences
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.)
Abandoned
Application number
CA002373135A
Other languages
English (en)
Inventor
Joerg M. Bentzien
Bassil I. Dahiyat
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.)
Xencor Inc
Original Assignee
Individual
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 Individual filed Critical Individual
Publication of CA2373135A1 publication Critical patent/CA2373135A1/fr
Abandoned legal-status Critical Current

Links

Classifications

    • D—TEXTILES; PAPER
    • D21—PAPER-MAKING; PRODUCTION OF CELLULOSE
    • D21C—PRODUCTION OF CELLULOSE BY REMOVING NON-CELLULOSE SUBSTANCES FROM CELLULOSE-CONTAINING MATERIALS; REGENERATION OF PULPING LIQUORS; APPARATUS THEREFOR
    • D21C5/00—Other processes for obtaining cellulose, e.g. cooking cotton linters ; Processes characterised by the choice of cellulose-containing starting materials
    • D21C5/005—Treatment of cellulose-containing material with microorganisms or enzymes
    • 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)
    • C12N9/24—Hydrolases (3) acting on glycosyl compounds (3.2)
    • C12N9/2402—Hydrolases (3) acting on glycosyl compounds (3.2) hydrolysing O- and S- glycosyl compounds (3.2.1)
    • C12N9/2477—Hemicellulases not provided in a preceding group
    • C12N9/248—Xylanases
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12Y—ENZYMES
    • C12Y302/00—Hydrolases acting on glycosyl compounds, i.e. glycosylases (3.2)
    • C12Y302/01—Glycosidases, i.e. enzymes hydrolysing O- and S-glycosyl compounds (3.2.1)
    • C12Y302/01008—Endo-1,4-beta-xylanase (3.2.1.8)
    • D—TEXTILES; PAPER
    • D21—PAPER-MAKING; PRODUCTION OF CELLULOSE
    • D21C—PRODUCTION OF CELLULOSE BY REMOVING NON-CELLULOSE SUBSTANCES FROM CELLULOSE-CONTAINING MATERIALS; REGENERATION OF PULPING LIQUORS; APPARATUS THEREFOR
    • D21C9/00—After-treatment of cellulose pulp, e.g. of wood pulp, or cotton linters ; Treatment of dilute or dewatered pulp or process improvement taking place after obtaining the raw cellulosic material and not provided for elsewhere
    • D21C9/10—Bleaching ; Apparatus therefor

Landscapes

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

Abstract

L'invention concerne de nouvelles protéines et acides nucléiques à activité de xylanase (XA) ainsi que l'utilisation des protéines XA dans le blanchiment de pâtes à papier.
CA002373135A 1999-05-12 2000-05-12 Nouvelle xylanase alcalinophile thermostable Abandoned CA2373135A1 (fr)

Applications Claiming Priority (3)

Application Number Priority Date Filing Date Title
US13371499P 1999-05-12 1999-05-12
US60/133,714 1999-05-12
PCT/US2000/013172 WO2000068396A2 (fr) 1999-05-12 2000-05-12 Nouvelle xylanase alcalinophile thermostable

Publications (1)

Publication Number Publication Date
CA2373135A1 true CA2373135A1 (fr) 2000-11-16

Family

ID=22459972

Family Applications (1)

Application Number Title Priority Date Filing Date
CA002373135A Abandoned CA2373135A1 (fr) 1999-05-12 2000-05-12 Nouvelle xylanase alcalinophile thermostable

Country Status (5)

Country Link
EP (1) EP1179075A2 (fr)
JP (1) JP2002543791A (fr)
AU (1) AU5132700A (fr)
CA (1) CA2373135A1 (fr)
WO (1) WO2000068396A2 (fr)

Families Citing this family (15)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
JP2002510966A (ja) 1997-04-11 2002-04-09 カリフォルニア・インスティテュート・オブ・テクノロジー 自動蛋白質デザインのための装置および方法
AU774334B2 (en) * 1998-10-16 2004-06-24 Xencor Protein design automation for protein libraries
US6403312B1 (en) 1998-10-16 2002-06-11 Xencor Protein design automatic for protein libraries
US20020048772A1 (en) 2000-02-10 2002-04-25 Dahiyat Bassil I. Protein design automation for protein libraries
US7315786B2 (en) 1998-10-16 2008-01-01 Xencor Protein design automation for protein libraries
EP3339434A1 (fr) 2000-03-08 2018-06-27 DuPont Nutrition Biosciences ApS Variants de xylanase
WO2002038746A2 (fr) * 2000-11-10 2002-05-16 Xencor Nouvelle xylanase alcalinophile thermostable
GB0121387D0 (en) * 2001-09-04 2001-10-24 Danisco Modified hydrolases
US20090142802A1 (en) 2005-03-22 2009-06-04 Novozymes A/S Polypeptides and nucleic acids encoding same
CN101952437B (zh) * 2007-10-03 2014-04-09 维莱尼姆公司 木聚糖酶、编码它们的核酸以及其制备和应用方法
CN104293747A (zh) 2008-12-23 2015-01-21 杜邦营养生物科学有限公司 具有木聚糖酶活性的多肽
WO2010129287A2 (fr) 2009-04-27 2010-11-11 The Board Of Trustees Of The University Of Illinois Enzymes de dégradation d'hémicellulose
RU2012137954A (ru) 2010-02-12 2014-03-20 Деквест Аг Способ отбелки целлюлозы
WO2016073610A1 (fr) * 2014-11-07 2016-05-12 Novozymes A/S Accelerateur de blanchiment a base de xylanase
CN109207498A (zh) * 2018-11-08 2019-01-15 上海市农业科学院 一种来自芽孢杆菌耐高温饲料用木聚糖酶的制备

Family Cites Families (3)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US5405769A (en) * 1993-04-08 1995-04-11 National Research Council Of Canada Construction of thermostable mutants of a low molecular mass xylanase
US5759840A (en) * 1996-09-09 1998-06-02 National Research Council Of Canada Modification of xylanase to improve thermophilicity, alkalophilicity and thermostability
JP2002510966A (ja) * 1997-04-11 2002-04-09 カリフォルニア・インスティテュート・オブ・テクノロジー 自動蛋白質デザインのための装置および方法

Also Published As

Publication number Publication date
JP2002543791A (ja) 2002-12-24
WO2000068396A2 (fr) 2000-11-16
EP1179075A2 (fr) 2002-02-13
AU5132700A (en) 2000-11-21
WO2000068396A3 (fr) 2001-03-08
WO2000068396A9 (fr) 2002-07-04

Similar Documents

Publication Publication Date Title
US6682923B1 (en) Thermostable alkaliphilic xylanase
CA2373135A1 (fr) Nouvelle xylanase alcalinophile thermostable
WO2002038746A9 (fr) Nouvelle xylanase alcalinophile thermostable
Davies et al. Structure of the Bacillus agaradherans family 5 endoglucanase at 1.6 Å and its cellobiose complex at 2.0 Å resolution
Fujimoto et al. Crystal structure of Streptomyces olivaceoviridis E-86 β-xylanase containing xylan-binding domain
Juge et al. XIP-I, a xylanase inhibitor protein from wheat: a novel protein function
Törrönen et al. Structural and functional properties of low molecular weight endo-1, 4-β-xylanases
Leggio et al. High resolution structure and sequence of T. aurantiacus Xylanase I: Implications for the evolution of thermostability in family 10 xylanases and enzymes with βα‐barrel architecture
Durand et al. Emergence of a subfamily of xylanase inhibitors within glycoside hydrolase family 18
Larson et al. First crystallographic structure of a xylanase from glycoside hydrolase family 5: implications for catalysis
de Souza et al. Engineering increased thermostability in the GH-10 endo-1, 4-β-xylanase from Thermoascus aurantiacus CBMAI 756
Jordan et al. Highly active β-xylosidases of glycoside hydrolase family 43 operating on natural and artificial substrates
Natesh et al. Crystal structure at 1.8 Å resolution and proposed amino acid sequence of a thermostable xylanase from Thermoascus aurantiacus
Spurway et al. Calcium protects a mesophilic xylanase from proteinase inactivation and thermal unfolding
Bhagwat et al. A comparative analysis of GH18 chitinases and their isoforms from Beauveria bassiana: An in-silico approach
Sato et al. Module–intron correlation and intron sliding in family F/10 xylanase genes
Contreras et al. Can constraint network analysis guide the identification phase of KnowVolution? A case study on improved thermostability of an endo-β-glucanase
Li et al. Improving alkaline stability of α-L-rhamnosidase from Aspergillus niger through computational strategy combines with folding free energy and binding free energy
Michaux et al. Structural insights into the acidophilic pH adaptation of a novel endo-1, 4-β-xylanase from Scytalidium acidophilum
Tu et al. Structural insights into the mechanisms underlying the kinetic stability of GH28 endo-polygalacturonase
Šuchová et al. Glucuronoxylan recognition by GH 30 xylanases: a study with enzyme and substrate variants
Madan et al. Sequence and structural features of subsite residues in GH10 and GH11 xylanases
Dodda et al. Computational approach for identification, characterization, three-dimensional structure modelling and machine learning-based thermostability prediction of xylanases from the genome of Aspergillus fumigatus
Mathur et al. Structural comparison, docking and substrate interaction study of modeled endo-1, 4-beta xylanase enzyme of Bacillus brevis
Wen et al. Highly efficient synergistic activity of an α-L-arabinofuranosidase for degradation of arabinoxylan in barley/wheat

Legal Events

Date Code Title Description
FZDE Discontinued