To understand the umami taste of fermented broad bean paste (FBBP) and explore the umami mechanism, eight peptides (PKALSAFK, NKHGSGK, SADETPR, EIKKAALDANEK, DALAHK, LDDGR, and GHENQR) were separated and identified via ultrafiltration, RP-HPLC, and UPLC-QTOF-MS/MS methods. Sensory experiments suggested that eight novel peptides showed umami/umami-enhancing and salt-enhancing functions. Significantly, the threshold of EIKKAALDANEK in aqueous solution exceeded that of most umami peptides reported in the past 5 years. The omission test further confirmed that umami peptides contributed to the umami taste of FBBP. Molecular docking results inferred that all peptides easily bind with Ser, Glu, His, and Asp residues in T1R3 through hydrogen bonds and electrostatic interactions. The aromatic interaction, hydrogen bond, hydrophilicity, and solvent-accessible surface (SAS) were the main interaction forces. This work may contribute to revealing the secret of the umami taste of FBBP and lay the groundwork for the efficient screening of umami peptides.
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