Taste characteristics and umami mechanism of novel umami peptides from hen egg proteins

Abstract

The study aimed to identify umami peptides from the hen egg proteins including ovotransferrin, ovalbumin, ovomucoid, and ovomucin using virtual enzymatic, molecular docking, electronic tongue analysis, and molecular dynamic simulation. The results showed that the interaction energy of DDNK, DLTK, and EHGK with the umami receptor T1R1/T1R3 was −124.3, −109.7, and −107.4 kcal/mol, respectively. The umami values for peptides DDNK, DLTK, and EHGK were 3.02 ± 0.33, 3.35 ± 0.24, and 4.19 ± 0.21, respectively, measured at the concentration of 0.1 mg/mL by electronic tongue. Molecular docking analysis indicated that residues Glu70, Gln278, and Asp147 might be the key amino acids within the T1R1/T1R3 binding site. Besides, molecular dynamics simulation revealed that the T1R1/T1R3 formed stable complexes with the umami peptides during the simulation. The work indicated that DDNK, DLTK, and EHGK may potentially serve as a good source of desirable umami peptides and can be used as the precursor of flavoring agent. • DDNK, DLTK, and EHGK were identified from hen egg white proteins. • The umami values for DDNK, DLTK, and EHGK were 3.02 ± 0.33, 3.35 ± 0.24, and 4.19 ± 0.21, respectively. • The umami peptides DDNK, DLTK, and EHGK formed stable complexes with the T1R1/T1R3. • DDNK, DLTK, and EHGK may serve as a good source of desirable umami peptides.