Insight into the mechanism of thermostabilization of GH10 xylanase from Bacillus sp. strain TAR-1 by the mutation of S92 to E. Issue 2 (28th January 2021)

• Record Type: Journal Article
• Authors: Suzuki, Manami; Takita, Teisuke; Kuwata, Kohei; Nakatani, Kota; Li, Tongyang; Katano, Yuta; Kojima, Kenji; Mizutani, Kimihiko; Mikami, Bunzo; Yatsunami, Rie; Nakamura, Satoshi; Yasukawa, Kiyoshi
• Is Part Of: Bioscience, biotechnology, and biochemistry. Volume 85:Issue 2(2021)
• Page Start: 386
• Page End: 390
• Publication Date: 2021-01-28
• Subjects: GH10 -- xylanase -- thermostabilization -- thermodynamic analysis -- crystallographic analysis; Biotechnology -- Periodicals; Biochemistry -- Periodicals; 660.6
• DOI: 10.1093/bbb/zbaa003
• Languages: English
• ISSNs: 0916-8451

Abstract

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.