| 论文题目: | Cloning, expression and characterization of a novel salt-tolerant xylanase from Bacillus sp SN5 |
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| 作者: | Bai, WQ; Xue, YF; Zhou, C; Ma, YH |
| 联系作者: | Ma, YH |
| 刊物名称: | BIOTECHNOLOGY LETTERS |
| 期: | 11 |
| 卷: | 34 |
| 页: | 2093-2099 |
| 年份: | 2012 |
| 影响因子: | 1.683 |
| 论文下载: | 下载地址 |
| 摘要: | A xylanase gene (xyn10A) was cloned from Bacillus sp. SN5 and expressed in Escherichia coli. It encoded a 348-residue polypeptide of similar to 45 kDa. The deduced amino acid sequence had 68 % identity with the endo-1,4-beta-xylanase from Paenibacillus lactis 154 that belonged to family 10 of the glycoside hydrolases. Purified recombinant Xyn10A had maximum activity at 40 degrees 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 degrees C and 29 % activity at 5 degrees 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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