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Article

Five mutations in N-terminus confer thermostability on mesophilic xylanase.

Biochemical and biophysical research communications - 30 Apr 2010

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

Abstract excerpt

The termini of a pair of xylanases, one of mesophilic and one of thermophilic origin, was studied by molecular dissection and systematic mutagenesis. The thermostability of the mesophilic xylanase SoxB from Streptomyces olivaceovirdis was significantly improved by substituting its 33 N-terminal amino acid residues with the corresponding residues of the thermophilic xylanase TfxA from Thermomonospora fusca. Five...

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Identifiers

PMID: 20361933
DOI: 10.1016/j.bbrc.2010.03.159

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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