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Inhibitory mechanism of catechins against advanced glycation end products of glycated myofibrillar protein through anti-aggregation and anti-oxidation

文献类型： 外文期刊

作者： Zhu, Zongshuai 1 ; Bassey, Anthony Pius 1 ; Khan, Iftikhar Ali 2 ; Huang, Ming 1 ; Zhang, Xibin 4 ;

作者机构： 1.Nanjing Agr Univ, Coll Food Sci & Technol, Nanjing 210095, Peoples R China

2.Jiangsu Acad Agr Sci, Inst Agr Prod Proc, Nanjing 210095, Peoples R China

3.Nanjing Huangjiaoshou Food Sci & Technol Co Ltd, Natl R&D Ctr Poultry Proc Technol, Nanjing 211200, Peoples R China

4.Shandong New Hope Liuhe Grp Co Ltd, Qual Control Feed & Prod Livestock & Poultry Key, Chengdu 610023, Sichuan, Peoples R China

关键词： Catechins; Advanced glycation end products; Myofibrillar protein; Anti-aggregation; Anti-oxidation

期刊名称：LWT-FOOD SCIENCE AND TECHNOLOGY （ 影响因子：4.952； 五年影响因子：5.383 ）

ISSN： 0023-6438

年卷期： 2021 年 147 卷

页码：

收录情况： SCI

摘要： Protein aggregation and oxidation could induce the generation of advanced glycation end products (AGEs). N epsilon carboxymethyl lysine (CML), N epsilon-carboxyethyllysine (CEL) are two typical AGEs markers in muscle foods. Catechins are considered to be excellent natural antioxidants for scavenging AGEs in muscle protein. We compared, for the first time, the inhibitory effects and explored mechanisms of (-)-epigallocatechin (EGC), (-)-epigallocatechin-3-gallate (EGCG), (-)-epicatechin (EC), and (-)-epicatechin-3-gallate (ECG), in glycated myofibrillar protein (MPG) by measuring AGEs level, Maillard reaction degree, particle size and anti-oxidation ability using microstructure, multispectral and molecular docking techniques. The results showed that catechins dosedependently inhibited AGEs in MPG through influencing lysine and free amino group, alleviating the Maillard reaction, detaching the particle size, affecting the protein-catechins interaction, relieving aggregates, and scavenging free radicals. The underlying mechanism behind the result indicated that catechins altered the structure information, SDS-PAGE bands, and the interaction sites of MPG via anti-aggregation and anti-oxidation. Particularly, EC and ECG showed weaker antioxidant ability than EGC and EGCG, EGCG exhibited a significant Pearson's correlation with the anti-oxidation and anti-aggregation of CML but no significant association with CEL. Overall, this study provides a theoretical insight into the applications of catechins to muscle foods as AGEs inhibitors.

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