Cloning, Expression, and Characterization of a New Xylanase from Alkalophilic Paenibacillus sp 12-11

文献类型： 外文期刊

第一作者： Zhao, Yanyu

作者： Zhao, Yanyu;Yang, Peilong;Zhao, Yanyu;Meng, Kun;Luo, Huiying;Shi, Pengjun;Huang, Huoqing;Bai, Yingguo;Yao, Bin

作者机构：

关键词： Alkaline xylanase;Paenibacillus sp.;Escherichia coli;protease resistance

期刊名称：JOURNAL OF MICROBIOLOGY AND BIOTECHNOLOGY （ 影响因子：2.351； 五年影响因子：2.65 ）

ISSN： 1017-7825

年卷期： 2011 年 21 卷 8 期

页码：

收录情况： SCI

摘要： A xylanase gene, xyn7c, was cloned from Paenibacillus sp. 12-11, an alkalophilic strain isolated from the alkaline wastewater sludge of a paper mill, and expressed in Escherichia coli. The full-length gene consists of 1,296 bp and encodes a mature protein of 400 residues (excluding the putative signal peptide) that belongs to the glycoside hydrolase family 10. The optimal of the purified recombinant XYN7C was found to be 8.0, and the enzyme had good pH adaptability at 6.5-8.5 and stability over a broad pH range of 5.0-11.0. XYN7C exhibited maximum activity at 55 degrees C and was thermostable at 50 degrees C and below. Using wheat arabinoxylan as the substrate, XYN7C had a high specific activity of 1,886 U/mg, and the apparent K-m and V-max values were 1.18 mg/ml and 1,961 mu mol/mg/min, respectively. XYN7C also had substrate specificity towards various xylans, and was highly resistant to neutral proteases. The main hydrolysis products of xylans were xylose and xylobiose. These properties make XYN7C a promising candidate to be used in biobleaching, baking, and cotton scouring processes.

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