Identification of Novel Umami Peptides from Low-Salt Dry-Cured Ham Skin and Revelation of the Umami Mechanism through Molecular Docking with T1R1/T1R3.

Dry-cured ham is highly favored by consumers due to its unique flavor, which is attributed to its various umami peptides. Four novel umami peptides were isolated from the skin of low-salt dry-cured ham. Sensory evaluations and electronic tongue analysis demonstrated that these peptides exhibited umami thresholds of 0.125-0.5 mg/mL. Molecular docking with the T1R1/T1R3 receptor gave binding energies ranging from -8.6 to -7.638 kcal/mol, demonstrating that hydrogen bonds and van der Waals forces represent the main forces involved in the binding of these peptides to the umami receptor. Hydrogen bonding significantly enhance the binding stability, while the van der Waals forces optimize the binding conformation to promote conduction of the umami signal. These findings confirm the presence of novel umami peptides in the skin of low-salt dry-cured ham, thereby enriching the umami peptide database and providing a theoretical basis for the high-value utilization of byproducts in livestock product processing.