Study on the relationship between structure and taste activity of the umami peptide of Stropharia rugosoannulata prepared by ultrasound

文献类型： 外文期刊

第一作者： Li, Wen

作者： Li, Wen;Li, Zhengpeng;Wang, Qian;Zhang, Jingsong;Yang, Yan;Li, Wen;Chen, Wanchao;Ma, Haile;Zhang, Zhong;Wu, Di;Wang, Jinbin

作者机构：

关键词： Stropharia rugosoannulata; Ultrasound; Umami peptide; Molecular docking; Structure-taste activity relationship

期刊名称：ULTRASONICS SONOCHEMISTRY （ 影响因子：9.336； 五年影响因子：8.772 ）

ISSN： 1350-4177

年卷期： 2022 年 90 卷

页码：

收录情况： SCI

摘要： Through virtual screening, electronic tongue verification, and molecular docking technology, the structure-taste activity relationship of 47 kinds of umami peptides (octapeptide -undecapeptide) from Stropharia rugosoannulata prepared by simultaneous ultrasonic-assisted directional enzymatic hydrolysis was analyzed. The umami pep-tides of S.rugosoannulata can form hydrogen bond interaction and electrostatic interaction with umami receptors T1R1/T1R3. The amino acid residues at the peptides' N-terminal and C-terminal play a vital role in binding with the receptors to form a stable complex. D, E, and R are the primary amino acids in the peptides that easily bind to T1R1/T1R3. The basic amino acid in the peptides is more easily bound to T1R1, and the acidic amino acid is more easily bound to T1R3. The active amino acid sites of the receptors to which the peptides bind account for 42%-65% of the total active amino acid residues in the receptors. ASP147 and ASP219 are the critical amino acid residues for T1R1 to recognize the umami peptides, and ARG64, GLU45, and GLU48 are the critical amino acid residues for T1R3 to recognize the umami peptides. The increase in the variety and quantity of umami peptides is the main reason for improving the umami taste of the substrate prepared by synchronous ultrasound -assisted directional enzymatic hydrolysis. This study provides a theoretical basis for understanding simultaneous ultrasound-assisted directional enzymatic hydrolysis for preparing umami peptides from S.rugosoannulata, enhancing the flavor of umami, and the relationship between peptide structure and taste activity.

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