Overexpression and characterization of a novel cold-adapted and salt-tolerant GH1 beta-glucosidase from the marine bacterium Alteromonas sp L82

文献类型： 外文期刊

第一作者： Sun, Jingjing

作者： Sun, Jingjing;Wang, Wei;Yao, Congyu;Dai, Fangqun;Zhu, Xiangjie;Liu, Junzhong;Hao, Jianhua;Sun, Jingjing;Wang, Wei;Yao, Congyu;Dai, Fangqun;Zhu, Xiangjie;Liu, Junzhong;Hao, Jianhua;Yao, Congyu;Zhu, Xiangjie;Hao, Jianhua

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关键词： beta-glucosidase; marine; Alteromonas; cold adaptation; salt tolerance

期刊名称：JOURNAL OF MICROBIOLOGY （ 影响因子：3.422； 五年影响因子：3.28 ）

ISSN： 1225-8873

年卷期： 2018 年 56 卷 9 期

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收录情况： SCI

摘要： A novel gene (bgl) encoding a cold-adapted beta-glucosidase was cloned from the marine bacterium Alteromonas sp. L82. Based on sequence analysis and its putative catalytic conserved region, Bgl belonged to the glycoside hydrolase family 1. Bgl was overexpressed in E. coli and purified by Ni2+ affinity chromatography. The purified recombinant beta-glucosidase showed maximum activity at temperatures between 25 degrees C to 45 degrees C and over the pH range 6 to 8. The enzyme lost activity quickly after incubation at 40 degrees C. Therefore, recombinant beta-glucosidase appears to be a cold-adapted enzyme. The addition of reducing agent doubled its activity and 2 M NaCl did not influence its activity. Recombinant beta-glucosidase was also tolerant of 700 mM glucose and some organic solvents. Bgl had a K-m of 0.55 mM, a V-max of 83.6 U/mg, a k(cat) of 74.3 s(-1) and k(cat)/K-m of 135.1 at 40 degrees C, pH 7 with 4-nitrophenyl-beta-D-glucopyranoside as a substrate. These properties indicate Bgl may be an interesting candidate for biotechnological and industrial applications.

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