Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/64938
Type: Artigo de periódico
Title: Enzymatic de-glycosylation of rutin improves its antioxidant and antiproliferative activities
Author: de Araujo, MEMB
Franco, YEM
Alberto, TG
Sobreiro, MA
Conrado, MA
Priolli, DG
Sawaya, ACHF
Ruiz, ALTG
de Carvalho, JE
Carvalho, PD
Abstract: Bioavailability and biological properties of flavonoid glycosides can be improved after the enzymatic hydrolysis of specific glycosyl groups. In this study, we evaluate the antioxidant and antiproliferative potential of rutin after enzymatic hydrolysis performed by alpha-L-rhamnosidases (hesperidinase from Penicillium sp. and naringinase from Penicillium decumbens) previously heated at 70 degrees C for 30 min to inactivate the undesirable beta-D-glucosidase activity. The highest in vitro antioxidant activity determined by DPPH radical scavenging was achieved with rutin hydrolyzed by hesperidinase. Rutin was predominantly bioconverted into quercetin-3-glucoside. There was no statistical difference between xanthine oxidase inhibition by rutin before and after hydrolysis. However, in vitro inhibitory activity against ten human tumor cell lines showed that hydrolyzed rutin exerted a more potent antiproliferative effect than quercetin and rutin on various cancer cell lines, specially glioma, and ovarian and breast adenocarcinomas. These results indicate that quercetin-3-glucoside could be a promising functional derivative obtained by rutin hydrolysis. (c) 2013 Elsevier Ltd. All rights reserved.
Subject: Quercetin-3-glucoside
Rutin
Antioxidant
Antiproliferative
alpha-L-Rhamnosidases
Hydrolysis
Country: Inglaterra
Editor: Elsevier Sci Ltd
Rights: fechado
Identifier DOI: 10.1016/j.foodchem.2013.02.127
Date Issue: 2013
Appears in Collections:Unicamp - Artigos e Outros Documentos

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