The present work focuses on PCs structural characteristics behind the inhibition of digestive enzymes, emphasizes on the digestive enzymes as α-glycosidase. α-amylase, lipase, pepsin, trypsin , and chymotrypsin. Polyphenols are known to form complexes with proteins leading to changes in the structural, functional and nutritional properties of both compounds. Some characteristics such as molecular weight, number and position of substitution, and glycosylation of flavonoids seem to be related to the inhibitory effect of polyphenolss; also, this effect seems to be different for carbohydrate-hydrolyzing enzymes and proteases and lipases. The digestive enzyme–polyphenols molecular interactions have shown that non-covalent binding, mostly by van der Waals forces, hydrogen binding, hydrophobic binding, and other electrostatic forces regulate them. These interactions were mainly associated to non-competitive type inhibitions of the enzymatic activities.
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