Gene cloning, expression, and characterization of a thermostable xylanase from Nesterenkonia xinjiangensis CCTCC AA001025

文献类型： 外文期刊

第一作者： Kui, Hong

作者： Kui, Hong;Luo, Huiying;Shi, Pengjun;Bai, Yingguo;Yuan, Tiezheng;Wang, Yaru;Yang, Peilong;Yao, Bin;Kui, Hong;Dong, Shouliang

作者机构：

关键词： Glycoside hydrolase (GH) family 11;Nesterenkonia xinjiangensis;Thermostability;Xylanase

期刊名称：APPLIED BIOCHEMISTRY AND BIOTECHNOLOGY （ 影响因子：2.926； 五年影响因子：2.685 ）

ISSN：

年卷期：

页码：

收录情况： SCI

摘要： An endo-β-1,4-xylanase-encoding gene, xyn11NX, was cloned from Nesterenkonia xinjiangensis CCTCC AA001025 and expressed in Escherichia coli. The gene encoded a 192-amino acid polypeptide and a putative 50-amino acid signal peptide. The deduced amino acid sequence exhibited a high degree of similarity with the xylanases from Streptomyces thermocyaneoviolaceus (68%) and Thermobifida fusca (66%) belonging to glycoside hydrolase family 11. After purification to homogeneity, the recombinant Xyn11NX exhibited optimal activity at pH 7.0 and 55 °C and remained stable at weakly acidic to alkaline pH (pH 5.0-11.0). The enzyme was thermostable, retaining more than 80% of the initial activity after incubation at 60 °C for 1 h and more than 40% of the activity at 90 °C for 15 min. The K _m and V _(max) values for oat spelt xylan and birchwood xylan were 16.08 mg ml~(-1) and 45.66 μmol min~(-1) mg~(-1) and 9.22 mg ml~(-1) and 16.05 μmol min~(-1) mg~(-1), respectively. The predominant hydrolysis products were xylobiose and xylotriose when using oat spelt xylan or birchwood xylan as substrate.

分类号： Q5

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