Taste mechanism of umami peptides from Chinese traditional fermented fish (Chouguiyu) based on molecular docking using umami receptor T1R1/ T1R3
文献类型： 外文期刊
作者： Yang, Daqiao 1 ; Li, Chunsheng 1 ; Li, Laihao 1 ; Chen, Shengjun 1 ; Hu, Xiao 1 ; Xiang, Huan 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.Jiangsu Ocean Univ, Coinnovat Ctr Jiangsu Marine Bioind Technol, Lianyungang 222005, Peoples R China
3.Ocean Univ China, Coll Food Sci & Engn, Qingdao 266003, Peoples R China
4.Dalian Polytech Univ, Collaborat Innovat Ctr Seafood Deep Proc, Dalian 116034, Peoples R China
关键词： Chouguiyu; Umami peptides; Precursor proteins; Molecular docking; Taste characteristics
期刊名称：FOOD CHEMISTRY （ 影响因子：9.231； 五年影响因子：8.795 ）
ISSN： 0308-8146
年卷期： 2022 年 389 卷
页码：
收录情况： SCI
摘要： Umami peptides formed during fermentation of Chouguiyu contribute to its unique taste. In this study, the umami taste of peptide extract from Chouguiyu was improved after fermentation, as determined by sensory evaluation. After umami peptide identification using peptidomics, molecular docking with T1R1/T1R3 was used to evaluate the likely taste mechanism. There were 400 umami peptides identified in Chouguiyu, most of which were significantly enhanced after fermentation. These peptides were hydrolyzed from 77 precursor proteins, mainly including myosin, troponin, and titin, at multiple locations. The umami structures in the six core umami peptides with the lowest binding energy were easy to connect with Ser, Glu, His, Gln, Arg and Lys residues in T1R3 through hydrogen bond and salt bridge. The hydrogen bond, hydrophilcity, aromatic interaction, and solvent accessible surface were the main interaction surface forces. This study provides important information of the unique taste formation in Chouguiyu based on umami peptides.
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