A β-glucosidase from Novosphingobium sp GX9 with high catalytic efficiency toward isoflavonoid glycoside hydrolysis and (+)-catechin transglycosylation

被引：19

作者：

Du, Liqin ^{[1
]}

Wang, Zilong ^{[1
]}

Zhao, Yingli ^{[1
]}

Huang, Jinqun ^{[1
]}

Pang, Hao ^{[2
]}

Wei, Yutuo ^{[1
]}

Lin, Lihua ^{[2
]}

Huang, Ribo ^{[1
]}

机构：

[1] Guangxi Univ, Coll Life Sci & Technol, Key Lab, Minist Educ Microbial & Plant Genet Engn, Nanning 530005, Guangxi, Peoples R China

[2] Guangxi Acad Sci, Natl Engn Res Ctr Nonfood Biorefinery, Nanning 530007, Guangxi, Peoples R China

来源：

APPLIED MICROBIOLOGY AND BIOTECHNOLOGY | 2014年 / 98卷 / 16期

基金：

中国国家自然科学基金;

关键词：

Novosphingobium sp; beta-Glucosidase; Isoflavone glycosides; Transglycosylation; Catechin glycosides; MULTIPLE SEQUENCE ALIGNMENT; SUCROSE PHOSPHORYLASE; ALKYL-GLUCOSIDES; P-GLUCOSIDASE; TEMPERATURES; TOLERANCE; CAPACITY; CLONING; HUMANS;

D O I：

10.1007/s00253-014-5661-3

中图分类号：

Q81 [生物工程学（生物技术）]; Q93 [微生物学];

学科分类号：

071005 ; 0836 ; 090102 ; 100705 ;

摘要：

In view of the important role of isoflavonoids and their related glycoconjugates in human health, there is considerable interest in their enzymatic conversion. SBGL, a novel beta-glucosidase isolated from Novosphingobium sp. GX9, was expressed in Escherichia coli and found to have high activity for hydrolysis of daidzin and genistin. SBGL showed very low K (m) values for daidzin and genistin, and the k (cat)/K (m) values for these substrates were 33,300 and 19,200 s(-1) mM(-1), respectively. The SBGL glucosidase could also transglycosylate the flavanol (+)-catechin at saturating acceptor concentrations, which has not previously been reported for a beta-glucosidase and is difficult to achieve synthetically.

引用

页码：7069 / 7079

页数：11

共 35 条

[31] Hydrolysis of soy isoflavone glycosides by recombinant β-glucosidase from hyperthermophile Thermotoga maritima [J].