Salt is very important for human health and food seasoning. Recently, several peptides isolated from natural food products have been reported exhibiting a salty taste or a saltiness-enhancing function. In this investigation, taste-active peptides occurring in commercial Chinese fermented soybean curd were isolated and identified using ultrafiltration, gel permeation chromatography, ion-exchange chromatography, and nano-LC/Q-TOF MS/MS. The salty taste-enhancing function of the target fractions was confirmed by both a rat taste cell model and/or human sensory evaluation. Four decapeptides were found as taste-active compounds. Among them, peptide E (EDEGEQPRPF) was the most potent saltiness-enhancing peptide: 0.4 mg/mL in 50 mmol/L NaCl solution could increase its salty perception equivalent to the salt level of 63 mmol/L NaCl reference solution. The sequence of the peptide has been found in the α'-subunit of β-conglycinin [Glycine max]. The remaining peptides V (VGPDDDEKSW), DD (DEDEQPRPIP), and DG (DEGEQPRPFP) showed umami and kokumi tastes as well as a weak saltiness-enhancing sensation. These findings suggest that the decapeptide EDEGEQPRPF could be a possible alternative to partially reduce the amount of sodium intake without compromising for saltiness.
Keywords: chromatography; fermented soybean curd; salty taste-enhancing peptides; sensory evaluation; sodium reduction.