A novel salt-tolerant GH42 beta-galactosidase with transglycosylation activity from deep-sea metagenome

文献类型： 外文期刊

第一作者： Sun, Jingjing

作者： Sun, Jingjing;Yao, Congyu;Wang, Wei;Hao, Jianhua;Sun, Jingjing;Wang, Wei;Hao, Jianhua;Yao, Congyu;Li, Yujie;Hao, Jianhua;Yu, Yi

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关键词： beta-Galactosidase; Metagenome; Lactose; Transglycosylation; Salt tolerance

期刊名称：WORLD JOURNAL OF MICROBIOLOGY & BIOTECHNOLOGY （ 影响因子：4.253； 五年影响因子：4.272 ）

ISSN： 0959-3993

年卷期： 2022 年 38 卷 9 期

页码：

收录情况： SCI

摘要： beta-Galactosidase is a widely adopted enzyme in the food and pharmaceutical industries. Metagenome techniques have the advantage of discovering novel functional genes, particularly potential genes from uncultivated microbes. In this study, a novel GH42 beta-galactosidase isolated from a deep-sea metagenome was overexpressed in Escherichia coli BL21 (DE3) and purified by affinity chromatography. The optimal temperatures and pH of the enzyme for o-nitrophenyl-beta-D-galactopyranoside (oNPG) and lactose were 40 degrees C, 6.5 and 50 degrees C, 7, respectively. The enzyme was stable at temperatures between 4 and 30 degrees C and within the pH range of 6-9. Moreover, it was highly tolerant to salt and inhibited by Zn2+ and Cu2+. The kinetic values of K-m and k(cat) of the enzyme against oNPG were 1.1 mM and 57.8 s(-1), respectively. Furthermore, it showed hydrolysis and transglycosylation activity to lactose and the extra monosaccharides could improve the productivity of oligosaccharides. Overall, this recombinant beta-galactosidase is a potential biocatalyst for the hydrolysis of milk lactose and synthesis of functional oligosaccharides.

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