14
views
0
recommends
+1 Recommend
0 collections
    0
    shares
      • Record: found
      • Abstract: found
      • Article: not found

      Grape seed and tea extracts and catechin 3-gallates are potent inhibitors of α-amylase and α-glucosidase activity.

      Read this article at

      ScienceOpenPublisherPubMed
      Bookmark
          There is no author summary for this article yet. Authors can add summaries to their articles on ScienceOpen to make them more accessible to a non-specialist audience.

          Abstract

          This study evaluated the inhibitory effects of plant-based extracts (grape seed, green tea, and white tea) and their constituent flavan-3-ol monomers (catechins) on α-amylase and α-glucosidase activity, two key glucosidases required for starch digestion in humans. To evaluate the relative potency of extracts and catechins, their concentrations required for 50 and 90% inhibition of enzyme activity were determined and compared to the widely used pharmacological glucosidase inhibitor, acarbose. Maximum enzyme inhibition was used to assess relative inhibitory efficacy. Results showed that grape seed extract strongly inhibited both α-amylase and α-glucosidase activity, with equal and much higher potency, respectively, than acarbose. Whereas tea extracts and catechin 3-gallates were less effective inhibitors of α-amylase, they were potent inhibitors of α-glucosidase. Nongallated catechins were ineffective. The data show that plant extracts containing catechin 3-gallates, in particular epigallocatechin gallate, are potent inhibitors of α-glucosidase activity and suggest that procyanidins in grape seed extract strongly inhibit α-amylase activity.

          Related collections

          Author and article information

          Journal
          J. Agric. Food Chem.
          Journal of agricultural and food chemistry
          1520-5118
          0021-8561
          Sep 12 2012
          : 60
          : 36
          Affiliations
          [1 ] Linus Pauling Institute, Oregon State University, Corvallis, Oregon 97331, USA.
          Article
          NIHMS599666
          10.1021/jf301147n
          22697360
          c551aacb-a097-40d1-9a13-7ff30bc76592
          History

          Comments

          Comment on this article