Revealing the Secret of Umami Taste of Peptides Derived from Fermented Broad Bean Paste

Abstract

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.

Identification of Novel Umami Peptides in Termitornyces albuminosus (Berk) Heim Soup by In Silico Analyses Combined with Sensory Evaluation: Discovering Potential Mechanism of Umami Taste Formation with Molecular Perspective

“…It is reported that the Venus flytrap domain (VFTD) of the T1R1 subunit is an active cavity, which is thought to be the main structure of taste recognition. 5 As shown in Figure 2, the molecular docking results between umami peptides and the receptor T1R1/T1R3 showed that these four umami peptides would bind to VFTD. To further accurately estimate the strength of the binding effect of peptides and T1R1, it is necessary to analyze the other interaction forces of peptides and T1R1 in addition to comparing the affinity energy.…”

“…It is reported that the Venus flytrap domain (VFTD) of the T1R1 subunit is an active cavity, which is thought to be the main structure of taste recognition . As shown in Figure , the molecular docking results between umami peptides and the receptor T1R1/T1R3 showed that these four umami peptides would bind to VFTD.…”

“…However, not all umami peptides contain these amino acids . Proline (P), histidine (H), valine (V), isoleucine (I), and leucine (L) also contribute to umami production . The molecular weights of these peptides (4 to 9 peptides) identified from T. albuminosus soup were less than 1500 Da, and all of these peptides contained the amino acid residues related to umami.…”

“…The umami taste of umami peptides is closely related to the peptide chain length, molecular weight, and type of 8,30 In general, these umami peptides have molecular weights less than 1500 Da and contain aspartic acid (D), glutamic acid (E), glutamine (Q), or asparagine (N). 5 However, not all umami peptides contain these amino acids. 30 Proline (P), histidine (H), valine (V), isoleucine (I), and leucine (L) also contribute to umami production.…”

Identifying Umami Peptides Specific to the T1R1/T1R3 Receptor via Phage Display

“…Umami peptides are small peptides with molecular weight ranging from 300 to 3000 Da, derived from various food sources, and these peptides possess multiple taste-presenting properties and nutritional value. − In recent years, umami peptides have received considerable attention as a crucial flavor regulator due to its umami or enhancing effects, making it a novel taste component. , The traditional methods for obtaining umami peptides involve extraction through thermal or enzymatic treatment, which is then followed by meticulous separation and purification using ultrafiltration and chromatography . However, the traditional screening sources are mainly from foods and rely strongly on the human sensory for stepwise screening, making the process more time-consuming and laborious.…”