Novel Umami Peptides from Hypsizygus marmoreus and Interaction with Umami Receptor T1R1/T1R3

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.

Automated summary

Umami peptides from Hypsizygus marmoreus hydrolysate were purified and identified. Their binding mechanism with T1R1/T1R3 receptor was investigated using computational simulations. Five novel umami peptides were obtained and their interaction forces with the receptor were analyzed. These findings contribute to the development of umami peptides in edible mushrooms.