Identification and taste characteristics of novel umami peptides from Yanjin black bone chicken hydrolysates and their binding mechanism with umami receptor

. Circular dichroism (CD) analysis indicated the presence of β-sheet structures in the umami peptides that could be associated with taste formation. In addition, molecular docking and molecular dynamics (MD) were employed to investigate the binding mechanisms between umami peptides and the umami receptor T1R1/T1R3. The findings reveal that Lys155, Arg255, and Gln250 of T1R1/T1R3 potentially play critical roles in umami peptide binding. Taken together, our results lay a foundation for researching flavor substances and for developing flavor products from Yanjin black bone chicken.