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

Authors :: Suzuki M
Takita T
Kuwata K
Nakatani K
Li T
Katano Y
Kojima K
Mizutani K
Mikami B
Yatsunami R
Nakamura S
Yasukawa K
Source :: Bioscience, biotechnology, and biochemistry [Biosci Biotechnol Biochem] 2021 Feb 18; Vol. 85 (2), pp. 386-390.
Publication Year :: 2021
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.<br /> (© The Author(s) 2021. Published by Oxford University Press on behalf of Japan Society for Bioscience, Biotechnology, and Agrochemistry.)

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

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