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
作者： Chen, Jieqiong 1 ; Lin, Chunyan 1 ; Yang, Lijia 1 ; Liu, Yang 3 ; Su, Guowan 2 ; Zhang, Yehui 1 ; Liu, Weifeng 1 ; Zhao, Mouming 2 ; Zhao, Xuan 4 ; Huang, Lihua 5 ; Zhao, Tiantian 1 ;
作者机构： 1.Minist Agr & Rural Affairs, Sericulture & Agrifood Res Inst Guangdong Acad Agr, Key Lab Funct Foods, Guangdong Key Lab Agr Prod Proc, Guangzhou 510610, Peoples R China
2.South China Univ Technol, Sch Food Sci & Engn, Guangzhou 510640, Peoples R China
3.Hunan Agr Univ, Coll Food Sci & Technol, Changsha 410128, Peoples R China
4.Guangdong AIB Polytech Coll, Guangzhou 510507, Guangdong, Peoples R China
5.Guangzhou City Polytech, Sch Food Hlth, Guangzhou 510405, Guangdong, Peoples R China
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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