Abstract
This study investigated the inhibition mechanism of cinnamic acid-based phenolic acids (cinnamic acid: CIA, 3,4-dimethoxy cinnamic acid: 3,4-mCIA, caffeic acid: CA, ferulic acid: FA) on starch digestion. CA, FA, and 3,4-mCIA contributed to reducing the rapidly digested starch content and increasing the resistant starch content. The enzyme activity inhibition results responded that the four phenolic acids inhibited α-amylase activity better than α-glucosidase. The order of IC50 against α-amylase and α-glucosidase was CA > FA > 3,4-mCIA > CIA. Phenolic acid's benzene ring formed conjugated Pi-systems with the amino acid residues of α-amylase. Salt-bridge interactions were the main driving forces for the binding of phenolic acids to α-glucosidase. The binding was stabilized by the hydroxyl (OH) group and the methoxy on the benzene ring, where the OH exerted a better effect. These results illuminate the inhibition mechanism of starch digestion with cinnamic acid-based phenolic acids from an interaction perspective.
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