Deglycosylation of stilbene glucoside compounds improves inhibition of 3-hydroxy-3-methylglutaryl coenzyme a reductase and squalene synthase activities

Keun Tae Park; Jeong Keun Kim; Young Hee Lim

doi:10.1007/s10068-014-0088-2

Deglycosylation of stilbene glucoside compounds improves inhibition of 3-hydroxy-3-methylglutaryl coenzyme a reductase and squalene synthase activities

Keun Tae Park, Jeong Keun Kim, Young Hee Lim

Department of Public Health Sciences

Research output: Contribution to journal › Article

5 Citations (Scopus)

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).

Original language	English
Pages (from-to)	647-651
Number of pages	5
Journal	Food Science and Biotechnology
Volume	23
Issue number	2
DOIs	https://doi.org/10.1007/s10068-014-0088-2
Publication status	Published - 2014 Jan 1

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Keywords

deglycosylation
HMG-CoA reductase
squalene synthase
stilbene

ASJC Scopus subject areas

Food Science
Biotechnology
Applied Microbiology and Biotechnology

Cite this

Park, K. T., Kim, J. K., & Lim, Y. H. (2014). Deglycosylation of stilbene glucoside compounds improves inhibition of 3-hydroxy-3-methylglutaryl coenzyme a reductase and squalene synthase activities. Food Science and Biotechnology, 23(2), 647-651. https://doi.org/10.1007/s10068-014-0088-2

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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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N2 - 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).

AB - 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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10.1007/s10068-014-0088-2