Abstract
Umami peptides are important taste components of foods. In this study, umami peptides from Hypsizygus marmoreus hydrolysate were purified through ultrafiltration, gel filtration chromatography, and RP-HPLC, and then identified using LC-MS/MS. The binding mechanism of umami peptides with the receptor, T1R1/T1R3, was investigated using computational simulations. Five novel umami peptides were obtained: VYPFPGPL, YIHGGS, SGSLGGGSG, SGLAEGSG, and VEAGP. Molecular docking results demonstrated that all five umami peptides could enter the active pocket in T1R1; Arg277, Tyr220, and Glu301 were key binding sites; and hydrogen bonding and hydrophobic interaction were critical interaction forces. VL-8 had the highest affinity for T1R3. Molecular dynamics simulations demonstrated that VYPFPGPL (VL-8) could be steadily packed inside the binding pocket of T1R1 and the electrostatic interaction was the dominant driving force of the complex (VL-8-T1R1/T1R3) formation. Arg residues (151, 277, 307, and 365) were important contributors to binding affinities. These findings provide valuable insights for the development of umami peptides in edible mushrooms.