Identification of Novel Umami Peptides in Chicken Breast Soup through a Sensory-Guided Approach and Molecular Docking to the T1R1/T1R3 Taste Receptor.

Abstract

Ultrafiltration combined with nanoliquid chromatography quadrupole time-of-flight mass spectrometry (nano-LC-QTOF-MS) and sensory evaluation was used to separate and identify umami peptides in chicken breast soup. Fifteen peptides with umami propensity scores of >588 were identified from the fraction (molecular weight ≤1 kDa) using nano-LC-QTOF-MS, and their concentrations ranged from 0.02 ± 0.01 to 6.94 ± 0.41 μg/L in chicken breast soup. AEEHVEAVN, PKESEKPN, VGNEFVTKG, GIQKELQF, FTERVQ, and AEINKILGN were considered as umami peptides according to sensory analysis results (detection threshold: 0.18-0.91 mmol/L). The measurement of point of subjective equality showed that these six umami peptides (2.00 g/L) were equivalent to 0.53-0.66 g/L of monosodium glutamate (MSG) in terms of umami intensity. Notably, the sensory evaluation results showed that the peptide of AEEHVEAVN significantly enhanced the umami intensity of the MSG solution and chicken soup models. The molecular docking results showed that the serine residues were the most frequently observed binding sites in T1R1/T1R3. The binding site Ser276 particularly contributed to the formation of the umami peptide-T1R1 complexes. The acidic glutamate residues observed in the umami peptides were also involved in their binding to the T1R1 and T1R3 subunits.