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Improvement mechanism of umami peptides in oyster juice by cooperative enzymolysis of alcalase and trypsin based on peptidomics and molecular docking

文献类型： 外文期刊

作者： Chen, Tianyu 1 ; Zhang, Fanxin 2 ; Chen, Shengjun 1 ; Zhao, Yongqiang 1 ; Huang, Xiaoqing 2 ; Huang, Feng 2 ; Li, Chunsheng 1 ;

作者机构： 1.Chinese Acad Fishery Sci, South China Sea Fisheries Res Inst, Natl R&D Ctr Aquat Prod Proc, Key Lab Aquat Prod Proc,Minist Agr & Rural Affairs, Guangzhou 510300, Peoples R China

2.Xianzhiran Guangdong Biotechnol Co Ltd, Foshan 528511, Peoples R China

3.Ocean Univ China, Coll Food Sci & Engn, Qingdao 266003, Peoples R China

关键词： Oyster juice; Cooperative enzymolysis; Free amino acid; Umami peptide; Peptidomics; Molecular docking

期刊名称：JOURNAL OF FOOD COMPOSITION AND ANALYSIS （ 影响因子：4.3； 五年影响因子：4.6 ）

ISSN： 0889-1575

年卷期： 2024 年 132 卷

页码：

收录情况： SCI

摘要： Traditional oyster juice is a by-product of dried oyster through stew of whole oyster, leading to few umami components from oyster. In this study, cooperative enzymolysis of alcalase and trypsin was used to improve the umami components of oyster juice. The optimal enzymolysis conditions of oyster juice included enzyme concentration of 0.4% alcalase and 0.1% trypsin, enzymolysis time of 1.5 h, and solid-liquid ratio of 1:8, and the amino acid nitrogen content in these conditions reached 0.53 g/L, obviously higher than that in non-enzymolysis group (0.27 g/L). The total free amino acids and peptides in the oyster juice were significantly improved by cooperative enzymolysis. After identification by peptidomics, 159 umami peptides were screened and 5 most abundant umami peptides were used to reveal the taste mechanism by molecular docking with the umami receptor T1R1/T1R3. Umami peptides mainly interacted with Arg56, Thr55, Glu48 and Arg64 in T1R3 through hydrogen attractive charge, conventional hydrogen bond, and carbon hydrogen bond, while hydrogen bond, interpolated charge, hydrophilicity, ionizability, and solvent accessible surface were the main surface forces. The "DED" structure in umami peptides was prone to interact with T1R3 receptor. This study provides a novel approach for enhancement of umami components in oyster juice.

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