Screening and identification of novel umami peptides from yeast proteins: Insights into their mechanism of action on receptors T1R1/T1R3.

This study aimed to unravel the peptide profiles of six distinct yeast protein samples and identify novel umami peptides within them. Peptide characteristics analysis support the proposition that yeast protein peptide pools represent exceptional reservoirs of umami peptides. Nine potential umami peptides were screened using the iUmami_SCM, UMPred-FRL, Umami_YYDS, Umami-MRNN, Innovagen, Expasy-ProtParam, and ToxinPred tools. Peptides AGVEDVY, LFEQHPEYRK, AFDVQ, GPTVEEVD, NVVAGSDLR, ATNGSR, and VEVVALND (1 mg/mL) were confirmed to possess umami taste, and the first five peptides exhibited significant umami-enhancing effects on 0.35 % monosodium glutamate. Molecular docking indicated that peptide residues His, Arg, Tyr, Asp, Gln, Thr, Ser, and Glu primarily bound to His71, Ser107/109/148, Asp147/218, and Arg277 of T1R1 and Ser104/146, His145, Asp216, Tyr218, and Ala302 of T1R3 through hydrogen bonds. This study enriches the umami peptide repository for potential food additive use and establishes a theoretical foundation for exploring taste compounds in yeast proteins and their broader applications. • Peptidomics analysis of six yeast proteins was conducted using nano-LC-MS/MS. • Seven of the nine virtually screened peptides exhibited a confirmed umami taste. • AGVEDVY, LFEQHPEYRK, AFDVQ, GPTVEEVD, and NVVAGSDLR had umami-enhancing effects. • Peptide residues H, R, Y, D, Q, T, S, E are mainly bound to receptors via H-bonds. • Residues H, S, D, R, Y in T1R1/3 are particularly vital for umami taste perception. [ABSTRACT FROM AUTHOR]