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Polypeptides having xylanase activity and polynucleotides encoding same

Patent ·
OSTI ID:1160253
The present invention relates to isolated polypeptides having xylanase activity and isolated polynucleotides encoding the polypeptides. The invention also relates to nucleic acid constructs, vectors, and host cells comprising the polynucleotides as well as methods of producing and using the polypeptides.
Research Organization:
Novozymes Inc., Davis, CA (United States)
Sponsoring Organization:
USDOE
DOE Contract Number:
FC36-08GO18080
Assignee:
Novozymes Inc. (Davis, CA)
Patent Number(s):
8,865,447
Application Number:
14/136,796
OSTI ID:
1160253
Country of Publication:
United States
Language:
English

References (12)

Protein tolerance to random amino acid change journal June 2004
Functional cloning of an endo-arabinanase from Aspergillus aculeatus and its heterologous expression in A. oryzae and tobacco journal July 2001
Stimulation of Lignocellulosic Biomass Hydrolysis by Proteins of Glycoside Hydrolase Family 61 Structure and Function of a Large, Enigmatic Family journal April 2010
Production of alkyl glucoside from cellooligosaccharides using yeast strains displaying Aspergillus aculeatus β-glucosidase 1 journal November 2007
Purification and Characterization of a New Endoglucanase from Aspergillus aculeatus journal September 2007
The Structure of an Inverting GH43 β-Xylosidase from Geobacillus stearothermophilus with its Substrate Reveals the Role of the Three Catalytic Residues journal May 2006
Cloning and transcription analysis of the Aspergillus aculeatus No. F-50 endoglucanase 2 (cmc2) gene journal January 2002
Microbial hemicellulases journal June 2003
Production of Aspergillus xylanase by lignocellulosic waste fermentation and its application: P. V. GAWANDE AND M. Y. KAMAT journal October 1999
Proteomic characterization of lignocellulose-degrading enzymes secreted by Phanerochaete carnosa grown on spruce and microcrystalline cellulose journal March 2010
Structural and Functional Analyses of β-Glucosidase 3B from Thermotoga neapolitana: A Thermostable Three-Domain Representative of Glycoside Hydrolase 3 journal April 2010
Glycoside hydrolases: Catalytic base/nucleophile diversity journal June 2010

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