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

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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.

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