Deglycosylation of stilbene glucoside compounds improves inhibition of 3-hydroxy-3-methylglutaryl coenzyme a reductase and squalene synthase activities
- Authors
- Park, Keun-Tae; Kim, Jeong-Keun; Lim, Young-Hee
- Issue Date
- Apr-2014
- Publisher
- KOREAN SOCIETY FOOD SCIENCE & TECHNOLOGY-KOSFOST
- Keywords
- stilbene; HMG-CoA reductase; squalene synthase; deglycosylation
- Citation
- FOOD SCIENCE AND BIOTECHNOLOGY, v.23, no.2, pp.647 - 651
- Indexed
- SCIE
SCOPUS
KCI
- Journal Title
- FOOD SCIENCE AND BIOTECHNOLOGY
- Volume
- 23
- Number
- 2
- Start Page
- 647
- End Page
- 651
- URI
- https://scholar.korea.ac.kr/handle/2021.sw.korea/98816
- DOI
- 10.1007/s10068-014-0088-2
- ISSN
- 1226-7708
- Abstract
- The glycosylated stilbenes mulberroside A and rhapontin were converted to their aglycones (oxyresveratrol and rhapontigenin) by enzymatic transformation. Rhapontin, rhapontigenin, mulberroside A, oxyresveratrol-3-O-glucoside, and oxyresveratrol showed inhibitory activities against 3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) reductase and squalene synthase, which are key enzymes in the cholesterol biosynthesis pathway. Aglycones showed stronger inhibitory activities than their glycosylated counterparts, and methoxylated stilbenes were stronger inhibitors of both enzymes than non-methoxylated stilbenes. The inhibitory activities of the stilbene compounds were significantly different from that of a negative control group (p < 0.05).
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Collections - College of Health Sciences > School of Biosystems and Biomedical Sciences > 1. Journal Articles
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