Identification and Taste Characteristics of Six Novel Umami Peptides from and Their Interaction with the T1R1/T1R3 Receptor.

is a commercially significant shellfish, highly regarded for its umami taste. In this study, umami taste peptides in were isolated and characterized through virtual screening, molecular docking, molecular dynamics simulations, sensory evaluation, and electronic tongue assessment. In silico enzymatic hydrolysis of myosin was performed, enabling the selection of six potential umami peptides (CR, ACR, GAR, PDL, PDPN, and SDADCF) based on predictions of umami taste, biological activity, toxicity, and water solubility. The interaction mechanisms between these peptides and the umami receptor T1R1/T1R3 were analyzed through molecular docking and dynamics simulations, revealing that SDADCF exhibited the most stable binding with T1R1/T1R3. The key residues of Asp, His, Glu, and Ser in T1R1 and T1R3 were identified as crucial active sites for umami peptide binding. Hydrogen bonding and electrostatic interactions were found to be the primary forces driving this binding. Furthermore, the umami taste of these peptides was validated using sensory evaluation, indicating that SDADCF had the most intense umami taste (umami score of 5.8) and a threshold of 0.25-0.99 mmol/L for the six peptides. Electronic tongue analysis further recognized the umami taste of the peptides. The identification of these six umami peptides contributes to a deep molecular basis of the strong umami taste within .