Cargando…

Characterization of Proanthocyanidins in Stems of Polygonum multiflorum Thunb as Strong Starch Hydrolase Inhibitors

Characterzation of polyphenolic compounds in the stems of P. multiflorum was conducted using HPLC, high resolution LC-MS and LC-MS(n). Proanthocyanidins in particular were isolated in 4.8% yield using solvent extraction followed by Sephadex LH-20 fractionation. HPLC analysis using a diol column reve...

Descripción completa

Detalles Bibliográficos
Autores principales: Wang, Hongyu, Song, Lixia, Feng, Shengbao, Liu, Yuancai, Zuo, Gang, Lai, Fuli, He, Guangyuan, Chen, Mingjie, Huang, Dejian
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2013
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6270252/
https://www.ncbi.nlm.nih.gov/pubmed/23429342
http://dx.doi.org/10.3390/molecules18022255
_version_ 1783376655099625472
author Wang, Hongyu
Song, Lixia
Feng, Shengbao
Liu, Yuancai
Zuo, Gang
Lai, Fuli
He, Guangyuan
Chen, Mingjie
Huang, Dejian
author_facet Wang, Hongyu
Song, Lixia
Feng, Shengbao
Liu, Yuancai
Zuo, Gang
Lai, Fuli
He, Guangyuan
Chen, Mingjie
Huang, Dejian
author_sort Wang, Hongyu
collection PubMed
description Characterzation of polyphenolic compounds in the stems of P. multiflorum was conducted using HPLC, high resolution LC-MS and LC-MS(n). Proanthocyanidins in particular were isolated in 4.8% yield using solvent extraction followed by Sephadex LH-20 fractionation. HPLC analysis using a diol column revealed oligomers (from dimer to nonamer) as minor components, with (epi)catechin monomeric units predominating, and oligomers with higher degree of polymerization being dominant. Thiolysis treatment of the proanthocyanidins using mercaptoacetic acid produced thioether derivatives of (epi)catechin as the major product and a mean value of the degree of polymerization of 32.6 was estimated from the ratio of terminal and extension units of the (epi)catechin. The isolated proanthocyanidins were shown to strongly inhibit α-amylase with an acarbose equivalence (AE) value of 1,954.7 µmol AE/g and inhibit α-glucosidase with an AE value of 211.1 µmol AE/g.
format Online
Article
Text
id pubmed-6270252
institution National Center for Biotechnology Information
language English
publishDate 2013
publisher MDPI
record_format MEDLINE/PubMed
spelling pubmed-62702522018-12-14 Characterization of Proanthocyanidins in Stems of Polygonum multiflorum Thunb as Strong Starch Hydrolase Inhibitors Wang, Hongyu Song, Lixia Feng, Shengbao Liu, Yuancai Zuo, Gang Lai, Fuli He, Guangyuan Chen, Mingjie Huang, Dejian Molecules Article Characterzation of polyphenolic compounds in the stems of P. multiflorum was conducted using HPLC, high resolution LC-MS and LC-MS(n). Proanthocyanidins in particular were isolated in 4.8% yield using solvent extraction followed by Sephadex LH-20 fractionation. HPLC analysis using a diol column revealed oligomers (from dimer to nonamer) as minor components, with (epi)catechin monomeric units predominating, and oligomers with higher degree of polymerization being dominant. Thiolysis treatment of the proanthocyanidins using mercaptoacetic acid produced thioether derivatives of (epi)catechin as the major product and a mean value of the degree of polymerization of 32.6 was estimated from the ratio of terminal and extension units of the (epi)catechin. The isolated proanthocyanidins were shown to strongly inhibit α-amylase with an acarbose equivalence (AE) value of 1,954.7 µmol AE/g and inhibit α-glucosidase with an AE value of 211.1 µmol AE/g. MDPI 2013-02-18 /pmc/articles/PMC6270252/ /pubmed/23429342 http://dx.doi.org/10.3390/molecules18022255 Text en © 2013 by the authors; licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/).
spellingShingle Article
Wang, Hongyu
Song, Lixia
Feng, Shengbao
Liu, Yuancai
Zuo, Gang
Lai, Fuli
He, Guangyuan
Chen, Mingjie
Huang, Dejian
Characterization of Proanthocyanidins in Stems of Polygonum multiflorum Thunb as Strong Starch Hydrolase Inhibitors
title Characterization of Proanthocyanidins in Stems of Polygonum multiflorum Thunb as Strong Starch Hydrolase Inhibitors
title_full Characterization of Proanthocyanidins in Stems of Polygonum multiflorum Thunb as Strong Starch Hydrolase Inhibitors
title_fullStr Characterization of Proanthocyanidins in Stems of Polygonum multiflorum Thunb as Strong Starch Hydrolase Inhibitors
title_full_unstemmed Characterization of Proanthocyanidins in Stems of Polygonum multiflorum Thunb as Strong Starch Hydrolase Inhibitors
title_short Characterization of Proanthocyanidins in Stems of Polygonum multiflorum Thunb as Strong Starch Hydrolase Inhibitors
title_sort characterization of proanthocyanidins in stems of polygonum multiflorum thunb as strong starch hydrolase inhibitors
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6270252/
https://www.ncbi.nlm.nih.gov/pubmed/23429342
http://dx.doi.org/10.3390/molecules18022255
work_keys_str_mv AT wanghongyu characterizationofproanthocyanidinsinstemsofpolygonummultiflorumthunbasstrongstarchhydrolaseinhibitors
AT songlixia characterizationofproanthocyanidinsinstemsofpolygonummultiflorumthunbasstrongstarchhydrolaseinhibitors
AT fengshengbao characterizationofproanthocyanidinsinstemsofpolygonummultiflorumthunbasstrongstarchhydrolaseinhibitors
AT liuyuancai characterizationofproanthocyanidinsinstemsofpolygonummultiflorumthunbasstrongstarchhydrolaseinhibitors
AT zuogang characterizationofproanthocyanidinsinstemsofpolygonummultiflorumthunbasstrongstarchhydrolaseinhibitors
AT laifuli characterizationofproanthocyanidinsinstemsofpolygonummultiflorumthunbasstrongstarchhydrolaseinhibitors
AT heguangyuan characterizationofproanthocyanidinsinstemsofpolygonummultiflorumthunbasstrongstarchhydrolaseinhibitors
AT chenmingjie characterizationofproanthocyanidinsinstemsofpolygonummultiflorumthunbasstrongstarchhydrolaseinhibitors
AT huangdejian characterizationofproanthocyanidinsinstemsofpolygonummultiflorumthunbasstrongstarchhydrolaseinhibitors