| Literature DB >> 25442950 |
Jin-A Ko1, J Y Park1, H J Kwon1, Y B Ryu1, H J Jeong1, S J Park1, C Y Kim1, H M Oh1, C S Park1, Y H Lim2, D Kim3, M C Rho1, W S Lee4, Y M Kim5.
Abstract
This study aimed to develop viable enzymes for bioconversion of resveratrol-glucoside into resveratrol. Out of 13 bacterial strains tested, Lactobacillus kimchi JB301 could completely convert polydatin into resveratrol. The purified enzyme had an optimum temperature of 30-40°C and optimum pH of pH 5.0 against polydatin. This enzyme showed high substrate specificities towards different substrates in the following order: isorhaponticin>>polydatin>>mulberroside A>oxyresveratrol-3-O-glucoside. Additionally, it rarely hydrolyzed astringin and desoxyrhaponticin. Based on these catalytic specificities, we suggest this enzyme be named stilbene glucoside-specific β-glucosidase. Furthermore, polydatin extracts from Polygonum cuspidatum were successfully converted to resveratrol with a high yield (of over 99%). Stilbene glucoside-specific β-glucosidase is the first enzyme isolated from lactic acid bacteria capable of bio-converting various stilbene glucosides into stilbene.Entities:
Keywords: Bioconversion; Lactobacillus kimchi; Polydatin ;·Resveratrol; β-Glucosidase
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Year: 2014 PMID: 25442950 DOI: 10.1016/j.enzmictec.2014.09.001
Source DB: PubMed Journal: Enzyme Microb Technol ISSN: 0141-0229 Impact factor: 3.493