Structural Insights into the Thermophilic Adaption Mechanism of Endo-1,4-beta-Xylanase from Caldicellulosiruptor owensensis
文献类型: 外文期刊
第一作者: Liu, Xin
作者: Liu, Xin;Xin, Fengjiao;Wen, Boting;Gu, Tianyi;Wang, Fengzhong;Sun, Lichao;Liu, Tengfei;Shi, Xinyuan;Zhang, Yuebin;Mi, Shuofu
作者机构:
关键词: GH10 xylanase;Caldicellulosiruptor owensensis;thermostability;crystal structure;Loop 7
期刊名称:JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY ( 影响因子:5.279; 五年影响因子:5.269 )
ISSN: 0021-8561
年卷期: 2018 年 66 卷 1 期
页码:
收录情况: SCI
摘要: Xylanases (EC 3.2.1.8) are a kind of enzymes degrading xylan to xylooligosaccharides (XOS) and have been widely used in a variety of industrial applications. Among them, xylanases from thermophilic microorganisms have distinct advantages in industries that require high temperature conditions. The CoXynA gene, encoding a glycoside hydrolase (GH) family 10 xylanase, was identified from thermophilic Caldicellulosiruptor owensensis and was overexpressed in Escherichia coli. Recombinant CoXynA showed optimal activity at 90 degrees C with a half-life of about 1 h at 80 degrees C and exhibited highest activity at pH 7.0. The activity of CoXynA activity was affected by a variety of cations. CoXynA showed distinct substrate specificities for beechwood xylan and birchwood xylan. The crystal structure of CoXynA was solved and a molecular dynamics simulation of CoXynA was performed. The relatively high thermostability of CoXynA was proposed to be due to the increased overall protein rigidity resulting from the reduced length and fluctuation of Loop 7.
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