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Article

Seven N-terminal residues of a thermophilic xylanase are sufficient to confer hyperthermostability on its mesophilic counterpart.

PloS one - 1 Jan 2014

Zhang Shan, He Yongzhi, Yu Haiying, Dong Zhiyang

Abstract excerpt

Xylanases, and especially thermostable xylanases, are increasingly of interest for the deconstruction of lignocellulosic biomass. In this paper, the termini of a pair of xylanases, mesophilic SoxB and thermophilic TfxA, were studied. Two regions in the N-terminus of TfxA were discovered to be potentially important for the thermostability. By focusing on Region 4, it was demonstrated that only two mutations, N32G...

Topics

Amino Acid Sequence
Endo-1,4-beta Xylanases
Escherichia coli
Molecular Sequence Data
Mutation
Recombinant Fusion Proteins
Sequence Homology, Amino Acid
Streptomyces
Temperature

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Identifiers

PMID: 24498158
DOI: 10.1371/journal.pone.0087632
PMCID: PMC3907472

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