化学
咖啡酸
加合物
共价键
赖氨酸
生物化学
多酚
半胱氨酸
凝胶电泳
组氨酸
免疫印迹
儿茶酚
氨基酸
聚丙烯酰胺凝胶电泳
有机化学
酶
抗氧化剂
基因
作者
Fenhong Yang,Yingying Zhu,Xiaohan Li,Fengtao Xiang,Mingtian Deng,Wei Zhang,Song Wu,Hao H. Sun,Changbo Tang
出处
期刊:Foods
[MDPI AG]
日期:2023-11-23
卷期号:12 (23): 4225-4225
标识
DOI:10.3390/foods12234225
摘要
Plant polyphenols with a catechol structure can form covalent adducts with meat proteins, which affects the quality and processing of meat products. However, there is a lack of fast and effective methods of characterizing these adducts and understanding their mechanisms. This study aimed to investigate the covalent interaction between myofibrillar protein (MP) and caffeic acid (CA), a plant polyphenol with a catechol structure, using molecular probe technology. The CA-MP adducts were separated via sodium dodecyl sulfate–polyacrylamide gel electrophoresis (SDS-PAGE) and detected via Western blot and LC-MS/MS analyses. The Western blot analysis revealed that various specific adducts were successfully enriched and identified as bands around 220 kDa, 45 kDa, and two distinct bands between 95 and 130 kDa. Combined with the LC-MS/MS analysis, a total of 51 peptides were identified to be CA-adducted, corresponding to 31 proteins. More than 80% of the adducted peptides carried one adducted site, and the rest carried two adducted sites. The adducted sites were located on cysteine (C/Cys), histidine (H/His), arginine (R/Arg), lysine (K/Lys), proline (P/Pro), and N-terminal (N-Term) residues. Results showed that the covalent interaction of CA and MP was highly selective for the R side chain of amino acids. Moreover, the adducts were more likely to form via C-N bonding than C-S bonding. This study provides new insights into the covalent interaction of plant polyphenols and meat proteins, which has important implications for the rational use of plant polyphenols in the meat processing industry.
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