Journal
FOODS
Volume 10, Issue 8, Pages -Publisher
MDPI
DOI: 10.3390/foods10081939
Keywords
maltase; sucrase; isomaltase; HPAE-PAD; polyphenols; quercetin; quercetagetin; kaempferol; galangin; acarbose
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Certain flavonoids have been found to influence glucose metabolism by inhibiting human alpha-glucosidases to different extents, with quercetagetin being the strongest inhibitor among the tested compounds. These compounds are more effective than EGCG but less so than acarbose, potentially playing a role in regulating sugar digestion and postprandial blood sugar levels.
Certain flavonoids can influence glucose metabolism by inhibiting enzymes involved in carbohydrate digestion and suppressing intestinal glucose absorption. In this study, four structurally-related flavonols (quercetin, kaempferol, quercetagetin and galangin) were evaluated individually for their ability to inhibit human alpha-glucosidases (sucrase, maltase and isomaltase), and were compared with the antidiabetic drug acarbose and the flavan-3-ol(-)-epigallocatechin-3-gallate (EGCG). Cell-free extracts from human intestinal Caco-2/TC7 cells were used as the enzyme source and products were quantified chromatographically with high accuracy, precision and sensitivity. Acarbose inhibited sucrase, maltase and isomaltase with IC50 values of 1.65, 13.9 and 39.1 mu M, respectively. A similar inhibition pattern, but with comparatively higher values, was observed with EGCG. Of the flavonols, quercetagetin was the strongest inhibitor of alpha-glucosidases, with inhibition constants approaching those of acarbose, followed by galangin and kaempferol, while the weakest were quercetin and EGCG. The varied inhibitory effects of flavonols against human alpha-glucosidases depend on their structures, the enzyme source and substrates employed. The flavonols were more effective than EGCG, but less so than acarbose, and so may be useful in regulating sugar digestion and postprandial glycaemia without the side effects associated with acarbose treatment.
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