Identification and virtual screening of novel umami peptides from dry-cured ham bone gelatin through molecular docking

This study aimed to identify novel umami peptides (UPs) from dry-cured ham bone gelatin (DHBG) and elucidated their umami mechanism. Gelatin was extracted from dry-cured ham bones using citric acid combined with pepsin with the yield of 13.52 %. Subsequently, DHBG was hydrolyzed using alkaline protease and flavorzyme. Through a combination of peptidomics and virtual screening techniques, two novel umami peptides, YDGE and EVGAP, were identified from the hydrolysate, with binding energies of −7.862 and − 7.861 kcal/mol, respectively. Molecular docking analysis indicated that both peptides could bind to the active site within the T1R3 subunit of the umami taste receptor, with hydrogen bonds as the predominant interaction forces. qPCR analysis showed that both peptides significantly upregulated ( P  < 0.05) mRNA expression of T1R1, T1R3, and their downstream effector PLCβ2 in STC-1 cells. Additionally, at a concentration range of 0.25 to 2 mg/mL, both synthetic peptides, similar to MSG, effectively induced increased intracellular Ca 2+ in STC-1 cells. These findings highlight the potential application of DHBG as a flavoring agent and offer perspectives on the mechanism of interaction between receptors and UPs.