A new xylanase from thermoacidophilic Alicyclobacillus sp A4 with broad-range pH activity and pH stability

文献类型： 外文期刊

第一作者： Bai, Yingguo

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

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关键词： pH stability;pH activity

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

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收录情况： SCI

摘要： We have identified a highly pH-adaptable and stable xylanase (XynA4) from the thermoacidophilic Alicyclobacillus sp. A4, a strain that was isolated from a hot spring in Yunnan Province, China. The gene (xynA4) that encodes this xylanase was cloned, sequenced, and expressed in Escherichia coli. It encodes a 338-residue polypeptide with a calculated molecular mass of 42.5 kDa. The deduced amino acid sequence is most similar to (53% identity) an endo-1,4-beta-xylanase from Geobacillus stearothermophilus that belongs to family 10 of the glycoside hydrolases. Purified recombinant XynA4 exhibited maximum activity at 55A degrees C and pH 7.0, had broad pH adaptability (> 40% activity at pH 3.8-9.4) and stability (retaining > 80% activity after incubation at pH 2.6-12.0 for 1 h at 37A degrees C), and was highly thermostable (retaining > 90% activity after incubation at 60A degrees C for 1 h at pH 7.0). These properties make XynA4 promising for application in the paper industry. This is the first report that describes cloning and expression of a xylanase gene from the genus Alicyclobacillus.

分类号： Q81

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