Research on the dynamic perception mechanisms of umami peptides within seasoning matrices

BACKGROUND: Understanding the perception mechanisms of umami peptides within complex food matrices is essential for the rational design of flavor profiles and the enhancement of product stability. This study systematically investigates these mechanisms under varying seasoning conditions, such as pH, salt and sugar. RESULTS: , respectively, were identified from tuna myoglobin using virtual hydrolysis and screening techniques. Fluorescence spectroscopy and molecular dynamics simulations revealed that seasoning matrices induce dynamic conformational changes in the peptides, which modulate their binding stability to the T1R1/T1R3 receptor. Specifically, ion-π interactions (affecting electrostatic interactions) and sugar-mediated hydration (influencing hydrogen bonding) play crucial roles in determining binding stability. Furthermore, peptides with higher charge density and a greater proportion of hydrophilic amino acids were more sensitive to seasoning conditions. Notably, this study identifies the key perception sites on the T1R1/T1R3 receptor (including Asp254, Ser101, Ser122 and Lys345) involved in umami peptide recognition. In addition, these peptides consistently produced stable and enhanced umami perception across various real food matrices, including soy sauce, fish sauce, miso and Knorr chicken bouillon. CONCLUSION: This study provides a comprehensive understanding of how seasoning matrices influence the dynamic perception mechanisms of umami peptides, offering valuable insights for optimizing flavor formulations.