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Details

Autor(en) / Beteiligte
Titel
Enzymatic de-glycosylation of rutin improves its antioxidant and antiproliferative activities
Ist Teil von
  • Food chemistry, 2013-11, Vol.141 (1), p.266-273
Ort / Verlag
Kidlington: Elsevier Ltd
Erscheinungsjahr
2013
Quelle
Access via ScienceDirect (Elsevier)
Beschreibungen/Notizen
  • •Optimisation of enzymatic activity for the production of quercetin-3-glucoside.•Hesperidinase allowed higher conversion rates than naringinase.•Quercetin-3-glucoside has higher antiproliferative activity than rutin or quercetin.•Quercetin-3-glucoside shows high antioxidant activity evaluated by the DPPH method. 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 α-l-rhamnosidases (hesperidinase from Penicillium sp. and naringinase from Penicillium decumbens) previously heated at 70°C for 30min to inactivate the undesirable β-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.

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