Article
Insight into the mechanism of thermostabilization of GH10 xylanase from Bacillus sp. strain TAR-1 by the mutation of S92 to E.
Bioscience, biotechnology, and biochemistry - 18 Feb 2021
Suzuki Manami, Takita Teisuke, Kuwata Kohei, Nakatani Kota, Li Tongyang, Katano Yuta, Kojima Kenji, Mizutani Kimihiko, Mikami Bunzo, Yatsunami Rie, Nakamura Satoshi, Yasukawa Kiyoshi
Abstract excerpt
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.
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