Cloning, Expression, and Characterization of a New Streptomyces sp S27 Xylanase for Which Xylobiose is the Main Hydrolysis Product

文献类型： 外文期刊

第一作者： Li, Ning

作者： Li, Ning;Shi, Pengjun;Yang, Peilong;Wang, Yaru;Luo, Huiying;Bai, Yingguo;Zhou, Zhigang;Yao, Bin

作者机构：

关键词： Streptomyces sp S27;Xylanase;Overexpression;Pichia pastoris;Xylobiose

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

ISSN： 0273-2289

年卷期： 2009 年 159 卷 2 期

页码：

收录情况： SCI

摘要： A xylanase gene, xynBS27, was cloned from Streptomyces sp. S27 and consisted of 693 bp encoding a 230-residue protein, including a putative 41-residue signal peptide. Belonging to the glycoside hydrolase family 11, XynBS27 exhibits the maximum identity (75.9%) to the xylanase from Streptomyces sp. zxy19. Recombinant XynBS27 was overexpressed in Pichia pastoris, and the xylanase activity was 7624.0 U/ml after high-cell-density fermentation in 3.7-L fermenter. The purified recombinant XynBS27 had a high specific activity of 3272.0 U/mg. The optimum temperature and pH for XynBS27 activity was 65 degrees C and pH 6.5, respectively. XynBS27 showed good pH stability and retained more than 80% of the maximum activity after incubation in buffers with pH ranging between 4.0 and 12.0 at 37 degrees C for 1 h. The main hydrolysis product of xylan by XynBS27 was xylobiose (>75%), which was good for human health derived from its ability to modulate the intestinal function. The attractive biochemical characteristics of XynBS27 suggest that it may be a good candidate in a variety of industrial applications.

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