Influence of catechin-PAYCS interactions on gastrointestinal structural and bioactivity stability: Key mechanisms in digestive enzymes inhibition
文献类型： 外文期刊
第一作者： Chen, Jieqiong
作者： Chen, Jieqiong;Lin, Chunyan;Yang, Lijia;Zhang, Yehui;Liu, Weifeng;Zhao, Tiantian;Chen, Jieqiong;Su, Guowan;Zhao, Mouming;Yang, Lijia;Liu, Yang;Zhao, Xuan;Huang, Lihua
作者机构：
关键词： Pentapeptide; Catechin; Non-covalent/covalent interaction; Acetylcholinesterase (AChE); Gastrointestinal digestion
期刊名称：FOOD CHEMISTRY （ 影响因子：9.8； 五年影响因子：9.7 ）
ISSN： 0308-8146
年卷期： 2025 年 490 卷
页码：
收录情况： SCI
摘要： Food-derived bioactive peptides often show instability during digestion, limiting their functional application. Polyphenols can enhance peptide stability via covalent or non-covalent interactions, influencing structure, activity, and digestion behavior. This study investigated catechin (CA) interactions with PAYCS (Pro-Ala-Tyr-CysSer) and their effects on digestive stability and enzyme modulation. Covalent (CA-PS) and non-covalent (CA/PS) complexes were prepared via alkaline and physical treatments. Spectroscopic analysis confirmed distinct binding modes, altering structural stability and fluorescence properties. SEM and particle size analysis revealed that CAPS formed a more stable network. Digestion studies demonstrated that CA/PS better resisted gastric digestion, while CA-PS exhibited greater stability in the intestine. Under simulated digestion conditions, CA/PS complexes use mixed-type pepsin inhibition to preserve structure in the stomach, while CA-PS employ competitive trypsin inhibition to retain activity in the intestine. These findings suggest polyphenol-peptide interactions modulate peptide digestion and functional activity, providing insights for enhancing bioactive peptide stability in functional foods.
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