High-throughput discovery of umami peptides from pork bone and elucidation of their molecular mechanism for umami taste perception.

This study endeavored to high-throughput identify umami peptides from pork bone. Pork bone protein extracts were hydrolyzed using proteinase K and papain, enzymes selected through computational proteolysis of pork type I collagen under the controlled conditions predicted by umami intensity-guided response surface analysis. Peptide sequences (GVNAMLRK, HWDRSNWF, PGRGCPGN, NLRDNYRF, PGWETYRK, GPGCKAGL, VAQWRKCL, GPTAANRM) in hydrolysates were virtually screened as potential umami peptides. Sensory evaluation confirmed that six of these peptides demonstrate a progressive increase in umami intensity. Molecular docking revealed that hydrophilic amino acids in umami peptides predominantly formed hydrogen bonds with T1R1/T1R3. Specifically, residues Thr, Asn, Lys, Ser and Glu of peptides mainly interacted with Ser107/148/276 of T1R1, and residues Tyr, Arg and Asp played crucial roles in binding to the Ser104/146 and His145 of T1R3. This study offers insights into the high-value utilization of pork bones and guides the development of umami peptides in various food proteins.