4.7 Article

Flavanol Polymerization Is a Superior Predictor of α-Glucosidase Inhibitory Activity Compared to Flavanol or Total Polyphenol Concentrations in Cocoas Prepared by Variations in Controlled Fermentation and Roasting of the Same Raw Cocoa Beans

Journal

ANTIOXIDANTS
Volume 8, Issue 12, Pages -

Publisher

MDPI
DOI: 10.3390/antiox8120635

Keywords

flavan-3-ol; procyanidin; alpha-glucosidase; melanoidin; Maillard reaction

Funding

  1. USDA AFRI [2017-67017-26783]
  2. Virginia Agricultural Experiment Station
  3. Hatch Program of the National Institute of Food and Agriculture, U.S. Department of Agriculture

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Raw cocoa beans were processed to produce cocoa powders with different combinations of fermentation (unfermented, cool, or hot) and roasting (not roasted, cool, or hot). Cocoa powder extracts were characterized and assessed for alpha-glucosidase inhibitory activity in vitro. Cocoa processing (fermentation/roasting) contributed to significant losses of native flavanols. All of the treatments dose-dependently inhibited alpha-glucosidase activity, with cool fermented/cool roasted powder exhibiting the greatest potency (IC50: 68.09 mu g/mL), when compared to acarbose (IC50: 133.22 mu g/mL). A strong negative correlation was observed between flavanol mDP and IC50, suggesting flavanol polymerization as a marker of enhanced alpha-glucosidase inhibition in cocoa. Our data demonstrate that cocoa powders are potent inhibitors of alpha-glucosidase. Significant reductions in the total polyphenol and flavanol concentrations induced by processing do not necessarily dictate a reduced capacity for alpha-glucosidase inhibition, but rather these steps can enhance cocoa bioactivity. Non-traditional compositional markers may be better predictors of enzyme inhibitory activity than cocoa native flavanols.

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