Identification and Characterization of Novel Umami Peptides from Protein Hydrolysates of and Their Interaction with T1R1/T1R3 Receptor.

The study aimed to explore umami peptides derived from protein hydrolysates of According to the electronic tongue and sensory evaluation, the ultrafiltration fractions (<3 kDa) of the protein hydrolysates exhibited the strongest umami taste. The overall flavor of the screened fractions was significantly improved after the Maillard reaction, based on the electronic nose and electronic tongue analyses, and the content of total free amino acid increased from 387.35 to 589.30 μg/mL. A total of 37 peptides with high confidence were identified from the fractions using LC-MS/MS. Additionally, two novel umami peptides were screened through bioinformatics and molecular docking, and their recognition threshold was 0.43 (EYPPLGRFA) and 0.52 mmol/L (TVIDAPGHRDFI), respectively. In addition, molecular docking analysis revealed that the key binding sites, such as Ser148, Leu51, Arg327, and Leu468 in T1R1/T1R3 contributed to docking, and hydrogen bonding and hydrophobic interactions were the dominant interaction forces between the two umami peptides and T1R1/T1R3 receptor. This study contributes to the development and utilization of in flavored foods.