Five mutations in N-terminus confer thermostability on mesophilic xylanase-Reference-Cited by-同舟云学术

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Five mutations in N-terminus confer thermostability on mesophilic xylanase

Published:2010-04 Issue:2 Volume:395 Page:200-206
ISSN:0006-291X
Container-title:Biochemical and Biophysical Research Communications
language:en
Short-container-title:Biochemical and Biophysical Research Communications

Author:

Zhang Shan,Zhang Kai,Chen Xiuzhen,Chu Xin,Sun Fei,Dong Zhiyang

Funder

National High Technology Research and Development Program

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry,Biophysics

Reference24 articles.

1. Xylanases, xylanase families and extremophilic xylanases;Collins;FEMS Microbiol. Rev.,2005

2. A classification of glycosyl hydrolases based on amino acid sequence similarities;Henrissat;Biochem. J.,1991

3. The endoxylanases from family 11: computer analysis of protein sequences reveals important structural and phylogenetic relationships;Sapag;J. Biotechnol.,2002

4. Engineering hyperthermostability into a GH11 xylanase is mediated by subtle changes to protein structure;Dumon;J. Biol. Chem.,2008

5. An additional aromatic interaction improves the thermostability and thermophilicity of a mesophilic family 11 xylanase: structural basis and molecular study;Georis;Protein Sci.,2000

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4. Enhancing the acid stability of the recombinant GH11 xylanase xynA through N-terminal substitution to facilitate its application in apple juice clarification;International Journal of Biological Macromolecules;2024-05

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