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

文献类型: 外文期刊

作者: Sun, Jingjing 1 ; Yao, Congyu 1 ; Li, Yujie 4 ; Wang, Wei 1 ; Hao, Jianhua 1 ; Yu, Yi 6 ;

作者机构: 1.Chinese Acad Fishery Sci, Yellow Sea Fisheries Res Inst, Key Lab Sustainable Dev Polar Fishery, Minist Agr & Rural Affairs, Qingdao 266000, Peoples R China

2.Qingdao Natl Lab Marine Sci & Technol, Lab Marine Drugs & Bioprod, Qingdao 266000, Peoples R China

3.Jiangnan Univ, State Key Lab Food Sci & Technol, Wuxi 214000, Jiangsu, Peoples R China

4.Shandong Univ Sci & Technol, Coll Safety & Environm Engn, Qingdao 266000, Peoples R China

5.Jiangsu Collaborat Innovat Ctr Exploitat & Utiliz, Lianyungang 222000, Peoples R China

6.Qingdao Univ, Affiliated Hosp, Qingdao 266000, Peoples R China

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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