Elucidating the umami mechanisms of peptides in chicken breast enzymatic hydrolysate through the integration of peptidomics, sensomics, and cell biology

This study aimed to quantitatively identify and characterize umami peptides from chicken breast enzymatic hydrolysatean integrated peptidomics-sensomics-cell biology approach. Through ultrafiltration and nano LC-Q-Exactive HF/MS and sensory analysis, peptides with molecular weights of less than 1 kDa were screened. Molecular docking revealed peptides GFAGDDAPR and DDHFL with strong binding affinities to T1R1/T1R3 receptors (docking energies: -8.8 to -9.8 kcal/mol), which showed substantial umami enhancement effects in sensory evaluations. Furthermore, cellular assays confirmed these peptides triggered calcium responses (ΔF/F 0 = 0.12±0.02) comparable to 200 mmol/L MSG, with synergistic combinations reaching ΔF/F 0 = 0.20±0.03. The findings provide a scientific basis for developing novel umami enhancers, aiding in the reduction of sodium content in foods while meeting consumer demands for healthier food options. • GFAGDDAPR and DDHFL were identified with strong umami-enhancing properties. • Combined peptidomics, sensomics and molecular docking to elucidate umami mechanism. • Constructed cellular model to confirm peptide activation of umami receptors.