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

Abstract

The study aimed to explore umami peptides derived from protein hydrolysates of Morchella esculenta. 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 Morchella esculenta in flavored foods.

Investigation of umami peptides and taste mechanisms in Agrocybe aegerita: based on sensory evaluation and molecular docking techniques

“…These findings indicate that the model was satisfactory, as over 90% of the points were found within the reasonable regions, and amino acid residues conserved a better conformational configuration. 7 In addition, the final active conformation of the heterodimer obtained in our study showed consistency with the modeling results obtained by Zhang et al 38 and Wang et al 39 Therefore, the above findings showed that the homology models possessed high reliability, which was then employed in molecular docking analysis.…”