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 › peer-review

7 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 Apr

Keywords

HMG-CoA reductase
deglycosylation
squalene synthase
stilbene

ASJC Scopus subject areas

Biotechnology
Food Science
Applied Microbiology and Biotechnology

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

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).",

keywords = "HMG-CoA reductase, deglycosylation, squalene synthase, stilbene",

author = "Park, {Keun Tae} and Kim, {Jeong Keun} and Lim, {Young Hee}",

note = "Funding Information: Acknowledgments This work (grant No. C0033118) was supported by Business for Cooperative R&D between Industry, Academy, and Research Institute funded Korea Small and Medium Business Administration in 2012. Copyright: Copyright 2014 Elsevier B.V., All rights reserved.",

year = "2014",

month = apr,

doi = "10.1007/s10068-014-0088-2",

language = "English",

volume = "23",

pages = "647--651",

journal = "Food Science and Biotechnology",

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T1 - Deglycosylation of stilbene glucoside compounds improves inhibition of 3-hydroxy-3-methylglutaryl coenzyme a reductase and squalene synthase activities

AU - Park, Keun Tae

AU - Kim, Jeong Keun

AU - Lim, Young Hee

N1 - Funding Information: Acknowledgments This work (grant No. C0033118) was supported by Business for Cooperative R&D between Industry, Academy, and Research Institute funded Korea Small and Medium Business Administration in 2012. Copyright: Copyright 2014 Elsevier B.V., All rights reserved.

PY - 2014/4

Y1 - 2014/4

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).

KW - HMG-CoA reductase

KW - deglycosylation

KW - squalene synthase

KW - stilbene

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EP - 651

JO - Food Science and Biotechnology

JF - Food Science and Biotechnology

SN - 1226-7708

IS - 2

ER -

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

Abstract

Keywords

ASJC Scopus subject areas

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