Improvement of the catalytic performance of a hyperthermostable GH10 xylanase from Talaromyces leycettanus JCM12802.

doi:10.1016/j.biortech.2016.10.003

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Article

Improvement of the catalytic performance of a hyperthermostable GH10 xylanase from Talaromyces leycettanus JCM12802.

Bioresource technology - 1 Dec 2016

Wang Xiaoyu, Huang Huoqing, Xie Xiangming, Ma Rui, Bai Yingguo, Zheng Fei, You Shuai, Zhang Bingyu, Xie Huifang, Yao Bin, Luo Huiying

Abstract excerpt

A xylanase gene of GH 10, Tlxyn10A, was cloned from Talaromyces leycettanus JCM12802 and expressed in Pichia pastoris. Purified recombinant TlXyn10A was acidic and hyperthermophilic, and retained stable over the pH range of 2.0-6.0 and at 90°C. Sequence analysis of TlXyn10A identified seven residues probably involved in substrate contacting. Three mutants (TlXyn10A_P, _N and _C) were then constructed by...

Topics

Amino Acid Sequence
Biocatalysis
Chromatography, Ion Exchange
Cloning, Molecular
Electrophoresis, Polyacrylamide Gel
Endo-1,4-beta Xylanases
Enzyme Stability
Glycosylation
Hydrolysis
Ions

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Kinetics

Metals

Molecular Dynamics Simulation

Mutation

Recombinant Proteins

Sequence Analysis, DNA

Structural Homology, Protein

Substrate Specificity

Source

Open in PubMed

Identifiers

PMID: 27723474
DOI: 10.1016/j.biortech.2016.10.003

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