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Title: Xylanases, nucleic acids encoding them and methods for making and using them

Patent ·
OSTI ID:1423291

The invention relates to enzymes having xylanase, mannanase and/or glucanase activity, e.g., catalyzing hydrolysis of internal .beta.-1,4-xylosidic linkages or endo-.beta.-1,4-glucanase linkages; and/or degrading a linear polysaccharide beta-1,4-xylan into xylose. Thus, the invention provides methods and processes for breaking down hemicellulose, which is a major component of the cell wall of plants, including methods and processes for hydrolyzing hemicelluloses in any plant or wood or wood product, wood waste, paper pulp, paper product or paper waste or byproduct. In addition, methods of designing new xylanases, mannanases and/or glucanases and methods of use thereof are also provided. The xylanases, mannanases and/or glucanases have increased activity and stability at increased pH and temperature.

Research Organization:
USDOE Office of Energy Efficiency and Renewable Energy (EE) (United States)
Sponsoring Organization:
USDOE
DOE Contract Number:
1435-04-03-CA-70224
Assignee:
BP Corporation North America Inc. (Houston, TX)
Patent Number(s):
RE46,733
Application Number:
PCT/US2008/072030
OSTI ID:
1423291
Resource Relation:
Patent File Date: 2015 Jun 05
Country of Publication:
United States
Language:
English

References (10)

Thermostable xylanase patent April 1998
Thermostable xylanase patent June 1999
Actinomadura xylanase sequences and methods of use patent August 1999
Phenolic acid esterases, coding sequences and methods patent April 2002
Microbially expressed xylanases and their use as feed additives and other uses patent-application September 2005
Process for preparing montelukast and salts thereof patent-application September 2007
The Use of Forced Protein Evolution to Investigate and Improve Stability of Family 10 Xylanases: The Production Of Ca2+-Independent Stable Xylanases journal September 2004
Using molecular techniques to identify new microbial biocatalysts journal June 1998
Stabilization of xylanase by random mutagenesis journal January 1993
Crystallographic and mutational analyses of an extremely acidophilic and acid-stable xylanase: biased distribution of acidic residues and importance of Asp37 for catalysis at low pH journal December 1998

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