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

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

SUBMITTER: Dong X 

PROVIDER: S-EPMC9955199 | biostudies-literature | 2023 Feb

REPOSITORIES: biostudies-literature