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

作者：Du, Liqin; Wang, Zilong; Zhao, Yingli; Huang, Jinqun; Pang, Hao; Wei, Yutuo; Lin, Lihua; Huang, Ribo^*

来源：Applied Microbiology and Biotechnology, 2014, 98(16): 7069-7079.

DOI：10.1007/s00253-014-5661-3

• Novosphingobium sp
• beta-Glucosidase
• Isoflavone glycosides
• Transglycosylation
• Catechin glycosides

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.

• 出版日期2014-8
• 单位广西科学院; 广西大学