Arginine-mediated inhibition of cathepsin L: A novel strategy to mitigate gel deterioration in fermented Cyprinus carpio L. surimi

文献类型： 外文期刊

第一作者： Hui, Fuyi

作者： Hui, Fuyi;Yu, Shan;Cen, Qin;Hu, Wenkang;Chen, Hongyan;Ren, Yanjie;Zeng, Xuefeng;Hui, Fuyi;Ying, Xiongmei;Yu, Shan;Cen, Qin;Hu, Wenkang;Zeng, Xuefeng;Zeng, Xuefeng;Hui, Fuyi;Yu, Shan;Cen, Qin;Hu, Wenkang;Chen, Hongyan;Ren, Yanjie;Zeng, Xuefeng

作者机构：

关键词： Fermentation; Molecular docking; Surimi gel; L-arginine; Cathepsin L

期刊名称：INNOVATIVE FOOD SCIENCE & EMERGING TECHNOLOGIES （ 影响因子：6.8； 五年影响因子：7.6 ）

ISSN： 1466-8564

年卷期： 2025 年 104 卷

页码：

收录情况： SCI

摘要： This study aimed to clarify the functional effects of L-arginine (Arg) on the quality improvement of fermented Cyprinus carpio L. surimi (FCS) gel and to uncover the underlying mechanisms. FCS was prepared from Cyprinus carpio L. and supplemented with 0.5 % Arg (w/w) based on the total surimi weight. The samples were then analyzed using texture profile analysis, microstructural imaging, untargeted metabolomics, homology modeling, molecular docking, and enzymatic assays. Arg significantly enhanced gel elasticity, hardness, cohesiveness, and chewiness by 3.16, 12.27, 15.33, and 15.40 %, respectively, and improved water-holding capacity by 20.4 %. Microstructural analysis revealed a more compact and uniform gel network, associated with increased hydrogen and disulfide bonding and reduced hydrophobic interactions. Metabolomic profiling identified 510 differential metabolites, indicating alterations in pyrimidine, glycerolipid, and beta-alanine metabolism. Molecular docking showed that Arg formed stable hydrogen bonds and electrostatic interactions with cathepsin L (CPL), with a binding energy of-144.39 kcal/mol. Enzymatic validation further confirmed a 94.74 % inhibition of CPL activity, suggesting Arg effectively suppressed proteolysis and promoted protein network formation. Sensory analysis indicated that the addition of 0.5 % Arg enhanced the umami flavor. Molecular docking further supported these findings by demonstrating that Arg had a strong binding affinity with umami taste receptors, with a binding energy of-125.97 kcal/mol. These findings demonstrated that Arg significantly improved the structural and functional qualities of FCS gel, which collectively supports its potential as a safe, cost-effective, and multifunctional additive for surimi-based product development.

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