Polyphenolic Compounds and Digestive Enzymes: In Vitro Non-Covalent Interactions

Abstract

The digestive enzymes–polyphenolic compounds (PCs) interactions behind the inhibition of these enzymes have not been completely studied. The existing studies have mainly analyzed polyphenolic extracts and reported inhibition percentages of catalytic activities determined by UV-Vis spectroscopy techniques. Recently, pure PCs and new methods such as isothermal titration calorimetry and circular dichroism have been applied to describe these interactions. The present review focuses on PCs structural characteristics behind the inhibition of digestive enzymes, and progress of the used methods. Some characteristics such as molecular weight, number and position of substitution, and glycosylation of flavonoids seem to be related to the inhibitory effect of PCs; also, this effect seems to be different for carbohydrate-hydrolyzing enzymes and proteases. The digestive enzyme–PCs 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. The present review emphasizes on the digestive enzymes such as α-glycosidase (AG), α-amylase (PA), lipase (PL), pepsin (PE), trypsin (TP), and chymotrypsin (CT). Existing studies conducted in vitro allow one to elucidate the characteristics of the structure–function relationships, where differences between the structures of PCs might be the reason for different in vivo effects.

The Role of Dietary Phenolic Compounds in Protein Digestion and Processing Technologies to Improve Their Antinutritive Properties

“…In contrast to other digestive enzymes, such as pancreatic α‐amylase, pancreatic lipase and α‐glucosidase, effect of polyphenol compounds on digestive protease activity have been barely studied (Martinez‐Gonzalez and others ). Li and others () investigated the effect of different number of hydroxyl groups in four flavonoids, quercetin, luteolin, kaempferol and apigenin, on their inhibition of trypsin activity.…”

Use of agro‐industrial residues as potent antioxidant, antiglycation agents, and α‐amylase and pancreatic lipase inhibitory activity

“…Molecular interactions between digestive enzymes and phenolic compounds are mostly by van der Waals forces, hydrogen binding, hydrophobic binding, and other electrostatic forces. These interactions were previously associated to noncompetitive type inhibitions (Li, Yang, Fei, Zhang, & Wu, ; Martinez‐Gonzalez et al, ; Shobana, Sreerama, & Malleshi, ; Wang, Dong, Zhang, Shao, & Liu, ; Wu et al, ; Yang & Kong, ). Wang et al () reported that grape proanthocyanidins inhibited porcine pancreatic lipase activity in a noncompetitively inhibiting manner.…”

Study of pancreatic lipase inhibition kinetics and LC–QTOF–MS‐based identification of bioactive constituents of Momordica charantia fruits

“…epigallocatechin) lower cholesterol level by inhibiting pancreatic lipase (Juhel et al, ). The efficacy of quercetin‐3‐xyloside and quercetin‐3‐glucoside in inhibiting the catalytic activity of PL was reported in the literature (Martinez‐Gonzalez et al, ). The dihydroflavonol derivatives, viz.…”