Sensoproteomic Discovery of Taste-Modulating Peptides and Taste Re-engineering of Soy Sauce

Abstract

Soy sauce, one of the most common Asian fermented foods, exhibits a distinctive savory taste profile. In the present study, targeted quantitation of literature-known taste compounds, calculation of dose-over-threshold factors, and taste re-engineering experiments enabled the identification of 34 key tastants. Following the sensoproteomics approach, 14 umami-, kokumi-, and saltenhancing peptides were identified for the first time, with intrinsic taste threshold concentrations in the range of 166−939 μmol/L and taste-modulating threshold concentrations ranging from 42 to 420 μmol/L. The lowest taste-modulating threshold concentrations were found for the leucyl peptide LDYY with an umami-and salt-enhancing threshold of 42 μmol/L. Addition of the 14 newly identified peptides to the taste recombinate (aRec Dipeptides ) increased the overall taste intensity and mouthfulness of the recombinate, and comparison with the authentic soy sauce confirmed the identification of all key tastants. Finally, these data as well as the quantitative profiling of several (non)-fermented foods highlight the importance of fermentation with respect to taste formation. On the basis of this knowledge, microorganisms with specific digestion patterns may be used to tailor the taste profile and especially the salt taste sensation of soy sauces.

Typical Umami Ligand-Induced Binding Interaction and Conformational Change of T1R1-VFT

“…Furthermore, there was no effect of the nonumami-tasting compounds (e.g., cyclamate, NaCl, sucrose, citric acid, and quinine sulfate) on the RFI of refolded T1R1-VFT (p > 0.05, Figure 1F). 34,35 Receptor protein T1R3-VFT expressed as inclusion bodies in an E. coli system displayed the active function and capable of binding ligands with a fluorescence quenching manner after solubilization and refolding, 13 which was quite similar to our results.…”

Bioactive and Sensory Di- and Tripeptides Generated during Dry-Curing of Pork Meat

“…Since di- and tripeptides are known to impart sensory properties [ 10 ], a better knowledge of the proteolytic phenomenon is essential to give an extra value to the product and produce regular batches. During dry-cured ham processing, muscle sarcoplasmic and myofibrillar proteins undergo an intense proteolysis by endogenous muscle peptidases, releasing large amounts of small peptides and free amino acids.…”

“…Indeed, the progressive shortening of larger peptides during the dry-curing of ham suggests the release of a wide variety of di- and tripeptides, which might play an essential role in taste development and bioactivity of the product. It is known that di- and tripeptides are far more bioavailable than larger peptides [ 15 ], besides which it has recently been revealed that di- and tripeptides often prove to be crucial for the intrinsic taste of foods, and they can impart taste-modulating properties [ 10 ].…”

Identifying Sequential Residue Patterns in Bitter and Umami Peptides

“…Given the impact of individual amino acids, the challenging question, then, is to understand the role of specific residue patterns in determining a peptide's taste via physicochemical properties such as hydrophobicity, polarity, and charge. With the discovery of new taste-relevant peptides in foods from various preparations 18 and progress in plant-based foods, this question is becoming more relevant. For example, if we design surrogate products from plant proteins, it would be useful to identify which short sequences of these proteins exhibit particular flavors.…”