Taste properties and mechanism of umami peptides from fermented goose bones based on molecular docking and molecular dynamics simulation using umami receptor T1R1/T1R3

[Display omitted] •Four novel umami peptides were screened out by prediction and molecular docking.•GETGEAGER showed the strongest ability to enhance umami in different food systems.•Glu, Ser, and Asp residues of T1R1/T1R3 were found in umami peptides and receptors.•The stability of peptides-T1R3 complexes was validated by molecular dynamics simulation. Umami peptides are valuable taste substances due to their exceptional taste and beneficial properties. In this study, purification of fermented goose bone broth was performed using continuous chromatography and sensory analysis, and after identification through nano-LC-MS/MS, four umami peptides were screened out by umami activity prediction and molecular docking, which are VGYDAE, GATGRDGAR, GETGEAGER, and GETGEAGERG derived from collagen. Sensory analysis indicated that they were also umami-enhancing, with thresholds ranging from 0.41 to 1.15 mmol/L, among which GER9 was the best. Combining the results of docking and molecular dynamics simulation, it was known that hydrogen bond and electrostatic interactions were vital in driving the umami formation. Moreover, Glu, Ser, and Asp of umami receptor T1R1/T1R3 were the key residues for the binding between four umami peptides and T1R1/T1R3. These findings provide novel insights into the high-value utilization of goose bones and offer profound theoretical guidance for understanding the umami mechanism.