Structural Insights into the Thermophilic Adaption Mechanism of Endo-1,4-β-Xylanase from Caldicellulosiruptor owensensis

• DOI: 10.1021/acs.jafc.7b03607
• Publication Date: 2017-12-13T17:26:36Z
• Authors: Xin Liu; Tengfei Liu; Yuebin Zhang; Fengjiao Xin; Shuofu Mi; Boting Wen; Tianyi Gu; Xinyuan Shi; Fengzhong Wang; Lichao Sun
• Keywords: Thermostability; Hydrolase

Xylanases (EC 3.2.1.8) are a kind of enzymes degrading xylan to xylooligosaccharides (XOS) and have been widely used in variety industrial applications. Among them, xylanases from thermophilic microorganisms distinct advantages industries that require high temperature conditions. The CoXynA gene, encoding glycoside hydrolase (GH) family 10 xylanase, was identified Caldicellulosiruptor owensensis overexpressed Escherichia coli. Recombinant showed optimal activity at 90 °C with half-life about 1 h 80 exhibited highest pH 7.0. affected by cations. substrate specificities for beechwood birchwood xylan. crystal structure solved molecular dynamics simulation performed. relatively thermostability proposed be due the increased overall protein rigidity resulting reduced length fluctuation Loop 7.