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.