Purification and functional characterization of the first stilbene glucoside-specific beta-glucosidase isolated from Lactobacillus kimchi
- Authors
- Ko, Jin-A.; Park, J. Y.; Kwon, H. J.; Ryu, Y. B.; Jeong, H. J.; Park, S. J.; Kim, C. Y.; Oh, H. M.; Park, C. S.; Lim, Y. H.; Kim, D.; Rho, M. C.; Lee, W. S.; Kim, Y. M.
- Issue Date
- 12월-2014
- Publisher
- ELSEVIER SCIENCE INC
- Keywords
- Bioconversion; Polydatin; Resveratrol; beta-Glucosidase; Lactobacillus kimchi
- Citation
- ENZYME AND MICROBIAL TECHNOLOGY, v.67, pp.59 - 66
- Indexed
- SCIE
SCOPUS
- Journal Title
- ENZYME AND MICROBIAL TECHNOLOGY
- Volume
- 67
- Start Page
- 59
- End Page
- 66
- URI
- https://scholar.korea.ac.kr/handle/2021.sw.korea/96588
- DOI
- 10.1016/j.enzmictec.2014.09.001
- ISSN
- 0141-0229
- 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 degrees 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 beta-glucosidase. Furthermore, polydatin extracts from Polygonum cuspidatum were successfully converted to resveratrol with a high yield (of over 99%). Stilbene glucoside-specific beta-glucosidase is the first enzyme isolated from lactic acid bacteria capable of bio-converting various stilbene glucosides into stilbene. (C) 2014 Elsevier Inc. All rights reserved.
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