Symbiotic Streptomyces sp. TN119 GH 11 xylanase: a new pH-stable, protease- and SDS-resistant xylanase

文献类型： 外文期刊

第一作者： Zhou, Junpei

作者： Zhou, Junpei;Shi, Pengjun;Zhang, Rui;Huang, Huoqing;Meng, Kun;Yang, Peilong;Yao, Bin

作者机构：

关键词： Longhorned beetles;pH stability;Protease resistance;Streptomyces sp TN119;Xylanase

期刊名称：JOURNAL OF INDUSTRIAL MICROBIOLOGY & BIOTECHNOLOGY （ 影响因子：3.346； 五年影响因子：3.426 ）

ISSN： 1367-5435

年卷期： 2011 年 38 卷 4 期

页码：

收录情况： SCI

摘要： A pH-stable and protease-resistant xylanase (XynB119) was identified from Streptomyces sp. TN119, a strain isolated from the gut luminal contents of longhorned beetle (Batocera horsfieldi) larvae. Using the GC TAIL-PCR method, the 1,026-bp coding gene (xynB119) with 67.3% GC content was successfully cloned and expressed in Escherichia coli. It encodes a 341-residue polypeptide with a calculated molecular mass of 35.9 kDa, including a putative 41-residue signal peptide, a catalytic domain of glycosyl hydrolase (GH) family 11, a short Gly/Pro-rich linker, and a family 2 cellulose-binding domain (CBM 2). The deduced amino acid sequence is most similar to (61.9% identity) an endo-1,4-beta-xylanase from Streptomyces thermoviolaceus OPC-520. Purified recombinant XynB119 exhibited peak activity at 50A degrees C and pH 7.0, remained stable over a broad pH range (retaining > 70% activity after incubation at pH 1.0-11.0 for 1 h at 37A degrees C without substrate), had strong protease resistance (retaining > 90% activity after proteolytic treatment at 37A degrees C for 1 h) and SDS resistance (at 100 mM). These properties make XynB119 promising for application in the feed industry and valuable for basic research. Compared to r-XynB119, the r-XynB119 derivative without CBM 2 and linker region (r-XynB119d) exhibited a decreased pH stability of > 25% at extreme pHs (pH 1.0-3.0 and pH 11.0-12.0).

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