Antarctic Krill‐Derived Umami Peptides With Bitter‐Masking Activity: Identification and Molecular Mechanism

This study systematically investigated the extraction and identification of umami peptides, as well as their mechanism for masking bitterness. The hydrolysate of Antarctic krill was isolated and purified, and umami components were identified through sensory evaluation and instrumental analysis. 12 potential umami peptides were obtained via virtual screening using databases. ERDWPEGRG, EHFETATRD, and DWPEGR were selected for functional validation based on molecular docking binding energy screening. The results showed that the three umami peptides had bitter taste inhibition efficiencies of 81.14%, 92.16%, and 93.02%. Molecular docking analysis revealed that the binding sites of the three umami peptides (Phe 76, Trp 89, Val 180) overlap with those of quinine sulfate, indicating that they exert their masking effect through competitive binding to the bitter taste receptor. This research will provide a theoretical basis for developing natural, safe bitterness-masking agents and advance the process of high-value utilization of Antarctic krill.