A new xylanase from thermoalkaline Anoxybacillus sp E2 with high activity and stability over a broad pH range

文献类型： 外文期刊

第一作者： Wang, Jianshe

作者： Wang, Jianshe;Bai, Yingguo;Yang, Peilong;Shi, Pengjun;Luo, Huiying;Meng, Kun;Huang, Huoqing;Yao, Bin;Wang, Jianshe;Yin, Jun

作者机构：

关键词： molecular weight;thermostability;pH range;amino acid sequence similarity

期刊名称：WORLD JOURNAL OF MICROBIOLOGY & BIOTECHNOLOGY （ 影响因子：3.312； 五年影响因子：3.58 ）

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年卷期：

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收录情况： SCI

摘要： A xylanase gene, xynE2, was cloned from thermoalkaline Anoxybacillus sp. E2 and was expressed in Escherichia coli BL21 (DE3). The gene consisted of 987 bp and encoded a 328-residue xylanase with a calculated molecular weight of 38.8 kDa. On the basis of amino acid sequence similarities, this enzyme was assigned as a member of glycoside hydrolase family 10. Purified recombinant XynE2 showed maximal activity at pH 7.8 and 65A degrees C, and was thermostable at 60A degrees C. The enzyme was highly active and stable over a broad pH range, showing more than 90% of maximal activity at pH 6.6-pH 8.6 and retaining more than 80% of activity at pH 4.6-pH 12.0, 37A degrees C for 1 h, respectively. These favorable properties make XynE2 a good candidate in the pulp and paper industries. This is the first report on gene cloning, expression and characterization of a xylanase from the genus Anoxybacillus.

分类号： Q93

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