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Molecules 2017, 22(4), 669; doi:10.3390/molecules22040669

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

1
Departamento de Ciencias Químico Biológicas, Instituto de Ciencias Biomédicas, Universidad Autónoma de Ciudad Juárez, Ciudad Juárez (32310), Mexico
2
Departamento de Bioquímica, Facultad de Medicina, Universidad Nacional Autónoma de México, México D.F. (04510), Mexico
*
Author to whom correspondence should be addressed.
Academic Editor: Paula Andrade
Received: 9 March 2017 / Revised: 18 April 2017 / Accepted: 19 April 2017 / Published: 22 April 2017
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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. View Full-Text
Keywords: polyphenolic compounds; structure; digestive enzymes; enzymatic inhibition; van der Waals forces; hydrogen binding; hydrophobic binding polyphenolic compounds; structure; digestive enzymes; enzymatic inhibition; van der Waals forces; hydrogen binding; hydrophobic binding
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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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MDPI and ACS Style

Martinez-Gonzalez, A.I.; Díaz-Sánchez, Á.G.; Rosa, L.A.; Vargas-Requena, C.L.; Bustos-Jaimes, I.; Alvarez-Parrilla, E. Polyphenolic Compounds and Digestive Enzymes: In Vitro Non-Covalent Interactions. Molecules 2017, 22, 669.

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