Insight into the mechanism of thermostabilization of GH10 xylanase from Bacillus sp. strain TAR-1 by the mutation of S92 to E

Biosci Biotechnol Biochem. 2021 Feb 18;85(2):386-390. doi: 10.1093/bbb/zbaa003.

Abstract

The mechanism of thermostabilization of GH10 xylanase, XynR, from Bacillus sp. strain TAR-1 by the mutation of S92 to E was investigated. Thermodynamic analysis revealed that thermostabilization was driven by the decrease in entropy change of activation for thermal inactivation. Crystallographic analysis suggested that this mutation suppressed the fluctuation of the amino acid residues at position 92-95.

Keywords: GH10; crystallographic analysis; thermodynamic analysis; thermostabilization; xylanase.

MeSH terms

  • Bacillus / enzymology*
  • Endo-1,4-beta Xylanases / chemistry
  • Endo-1,4-beta Xylanases / genetics*
  • Endo-1,4-beta Xylanases / metabolism*
  • Enzyme Stability
  • Models, Molecular
  • Mutant Proteins / chemistry
  • Mutant Proteins / genetics*
  • Mutant Proteins / metabolism*
  • Mutation*
  • Protein Conformation
  • Temperature*

Substances

  • Mutant Proteins
  • Endo-1,4-beta Xylanases