Cloning, expression and characterization of a novel salt-tolerant xylanase from Bacillus sp. SN5

被引：0
作者：
Wenqin Bai
Yanfen Xue
Cheng Zhou
Yanhe Ma
机构：
[1] Institute of Microbiology,National Engineering Lab for Industrial Enzymes
[2] Chinese Academy of Sciences,undefined
[3] Graduate University of the Chinese Academy of Sciences,undefined
来源：
Biotechnology Letters | 2012年 / 34卷
关键词：
sp. SN5; Cold-active; Halo-tolerant; Xylanase;
D O I：
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中图分类号：
学科分类号：
摘要：
A xylanase gene (xyn10A) was cloned from Bacillus sp. SN5 and expressed in Escherichia coli. It encoded a 348-residue polypeptide of ~45 kDa. The deduced amino acid sequence had 68 % identity with the endo-1,4-beta-xylanase from Paenibacilluslactis 154 that belonged to family 10 of the glycoside hydrolases. Purified recombinant Xyn10A had maximum activity at 40 °C and pH 7.0, with the specific activity of 105 U/mg and a Km of 0.6 mg/ml for beechwood xylan. Xyn10A retained more than 80 % activity between 25 and 45 °C and 29 % activity at 5 °C. It exhibited the highest activity (134 %) in 0.5 M NaCl and still retained 90 % activity in 2.5 M NaCl. It retained about 87 % activity after incubation in 2 M NaCl for 24 h. The cold-active and halo-tolerant properties of Xyn10A make it promising for application in the food industry, especially in the processing of saline food and sea food.
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页码：2093 / 2099
页数：6
相关论文
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