Identification of Novel Umami Peptides in Termitornyces albuminosus (Berk) Heim Soup by In Silico Analyses Combined with Sensory Evaluation: Discovering Potential Mechanism of Umami Taste Formation with Molecular Perspective.

In this study, 24 peptides were identified in Termitornyces albuminosus (Berk) Heim soup, 12 of which were predicted to possess an umami taste based on the BIOPEP-UWM or Umami-MRNN databases. Among these 12 peptides, four peptides (i.e., QNDF, QGGDF, EPVTLT, and EVNYDFGGK) exhibited the lowest affinity energy with the umami receptor type 1 member 1 (T1R1) subunit. Molecular docking and molecular dynamics simulation further confirmed the strong binding of these four umami peptides to the umami receptor T1R1/T1R3, with the EVNYDFGGK forming the most stable complex. After synthesizing the four peptides, their umami taste was validated through sensory and electronic tongue analyses with recognition thresholds ranging from 0.0938 to 0.3750 mmol/L. Notably, the EVNYDFGGK peptide displayed the strongest umami taste (recognition threshold, 0.0938 mmol/L). This study may contribute to the industrial development of T. albuminosus by providing a new understanding of the mechanism of its umami formation.