Isolation and screening of umami peptides from preserved egg yolk by nano-HPLC-MS/MS and molecular docking

The material basis leading to the rich umami flavor of preserved egg yolk is poorly understood. This study used nano-high-performance liquid chromatography - tandem mass spectrometry (nano-HPLC-MS/MS) to isolate, identify, and screen umami peptides from preserved egg yolk. Five novel umami peptides-AGFMPLP, APYSGY, PPMF, SLSSLMK, and VAMNPVDHPH-were identified. Molecular docking showed that Phe527 on the taste receptor T1R1/T1R3 (T1R1, taste receptor type 1 member 1; T1R3, taste receptor type 1 member 3) was the key interaction site. Hydrogen bonding, electrostatic interactions, and hydrophobic interactions were the main binding forces between T1R1/T1R3 and umami peptides. These results contribute to understanding the umami peptides in preserved egg yolk and the interaction mechanism between umami peptides and umami receptors.