Journal
APPLIED MICROBIOLOGY AND BIOTECHNOLOGY
Volume 98, Issue 16, Pages 7069-7079Publisher
SPRINGER
DOI: 10.1007/s00253-014-5661-3
Keywords
Novosphingobium sp; beta-Glucosidase; Isoflavone glycosides; Transglycosylation; Catechin glycosides
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Funding
- National Natural Science Foundation of China [31360369]
- Guangxi Academy of Sciences [12YJ25SW05, 13YJ22SW02]
- State Key Laboratory for Conservation and Utilization of Subtropical Agro-bioresources
- BaGui Scholars Program Foundation
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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.
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