Catechin Inhibits the Release of Advanced Glycation End Products during Glycated Bovine Serum Albumin Digestion and Corresponding Mechanisms In Vitro.

Abstract

Glycated proteins are the main source of dietary advanced glycation end products (AGEs). Glycated proteins are enzymatically hydrolyzed in the gastrointestinal tract, which releases more absorbable and smaller potentially harmful AGEs. This study investigated the inhibitory effect of catechin on AGE release from glycated bovine serum albumin (G-BSA) during gastrointestinal digestion. Catechin inhibited AGE release during gastrointestinal digestion, especially in the gastric digestion stage. Additionally, catechin altered these peptides in the small intestine by reducing G-BSA digestibility. The proposed mechanism involves interactions between catechin and G-BSA/digestive enzymes, inhibiting digestive enzyme activity and changing the conformation of G-BSA. Catechin reduced G-BSA β-sheet content and protected the helical conformation. Moreover, catechin enhanced the antioxidant capacity of G-BSA, which could attenuate postprandial oxidative stress in the gastrointestinal tract caused by the release of AGEs. This study improves our understanding of the nutritional and health effects of catechin on dietary AGEs during gastrointestinal digestion.