Sensoproteomics: A New Approach for the Identification of Taste-Active Peptides in Fermented Foods

Abstract

Aiming at the identification of the key bitter peptides in fermented foods, a new approach, coined "sensoproteomics", was developed and applied to fresh cheese samples differing in bitter taste intensity. By means of MPLC fractionation of the water-soluble cheese extracts in combination with taste dilution analysis, complex fractions with intense bitter taste were located and then screened by UPLC−MS/MS for the entire repertoire of ∼1600 candidate peptides, extracted from a literature meta-analysis on dairy products, by using a total of 120 selected reaction monitoring methods computed in silico. A total of 340 out of the 1600 peptides were found in the cheese samples, among which 17 peptides were identified as candidate bitter peptides by considering only peptides that were located in the bitter-tasting MPLC fractions (signal-to-noise ratio: ≥10) with a fold-change of ≥3 when comparing the less bitter to the more bitter cheese sample and that were validated by comparison with the synthetic reference peptides. While EIVPNS[phos]VEQK (α s1 -CN 70−78 ) and INTIASGEPT (κ-CN 122−131 ) did not exhibit any bitter taste up to 2000 μmol/L, 15 of the 17 target peptides showed bitter taste thresholds ranging from 30 (ARHPHPHLSFM, κ-CN 96−106 ) to 690 μmol/L (IQKEDVPS, α s1 -CN 81−88 ). Finally, quantitative peptide analysis followed by calculation of dose-overthreshold factors revealed a primary contribution of MAPKHKEMPFPKYPVEPF (β-CN 102−119 ) and ARHPHPHLSFM (κ-CN 96−106 ) to the perceived bitter taste of the fresh cheese samples. Finally, the evolution of the bitter peptides throughout two different fresh cheese manufacturing processes was quantitatively recorded.

The relevance of dipeptides and tripeptides in the bioactivity and taste of dry-cured ham

“…Names of the abbreviated proteins are given in Table 1 tripeptides by MS techniques is necessary in order to study the amount of peptide present in food, evaluate its bioavailability, and establish the dose needed to exert an in vivo effect in the case of bioactive peptides (Mora et al 2017). Moreover, the new sensoproteomics approach, which combines sensory evaluation with instrumental analysis, is very useful to identify the taste-active key peptides and monitor their evolution during food processing (Sebald et al 2018). Nonetheless, the small size and low concentration of peptides, complexity of the matrix sample, peptide interferences, and signal suppression due to the matrix effects make the peptidomics analysis rather complicated (Mora et al 2017).…”

Metaproteomics insights into traditional fermented foods and beverages

“…Metaproteomics has been applied to study the functional microorganisms and their interactions in TFFB. The contribution of microbially metabolized proteins to food taste should be identified from the perspectives of flavor and especially taste, such as the presence of peptides that contribute to bitterness in cheese (Sebald, Dunkel, Schafer, Hinrichs, & Hofmann, 2018). The analysis of the microbial community and flavor substances in TFFB microecology plays an important role in ensuring the quality of fermented food produced on a large scale (Tamang et al., 2020).…”

Sensopeptidomic Kinetic Approach Combined with Decision Trees and Random Forests to Study the Bitterness during Enzymatic Hydrolysis Kinetics of Micellar Caseins

“…Various factors can influence the appearance of undesirable flavours in protein enzymatic hydrolysates, such as the nature of protein substrate(s) and enzyme(s), the hydrolysis duration, the selected pH and the temperature conditions. Concerning the casein proteins, β-, αS1and κ-caseins produce the most bitter hydrolysates [5]. The causes for the bitterness were identified as early as 1970 by Fujimaki et al and Matoba et al [6,7] as being the presence of specific peptides rather than free amino acids in the protein hydrolysate.…”