Soybean (<i>Glycine max</i>) Protein Hydrolysates as Sources of Peptide Bitter-Tasting Indicators: An Analysis Based on Hybrid and Fragmentomic Approaches

Abstract

The aim of this study was to analyze soybean proteins as sources of peptides likely to be bitter using fragmentomic and hybrid approaches involving in silico and in vitro studies. The bitterness of peptides (called parent peptides) was theoretically estimated based on the presence of bitter-tasting motifs, particularly those defined as bitter-tasting indicators. They were selected based on previously published multilinear stepwise regression results. Bioinformatic-assisted analyses covered the hydrolysis of five major soybean-originating protein sequences using bromelain, ficin, papain, and proteinase K. Verification of the results in experimental conditions included soy protein concentrate (SPC) hydrolysis, RP-HPLC (for monitoring the proteolysis), and identification of peptides using RP-HPLC-MS/MS. Discrepancies between in silico and in vitro results were observed when identifying parent peptide SPC hydrolysate samples. However, both analyses revealed that conglycinins were the most abundant sources of parent peptides likely to taste bitter. The compatibility percentage of the in silico and in vitro results was 3%. Nine parent peptides with the following sequences were identified in SPC hydrolysates: LSVISPK, DVLVIPLG, LIVILNG, NPFLFG, ISSTIV, PQMIIV, PFPSIL, DDFFL, and FFEITPEK (indicators are in bold). The fragmentomic idea of research might provide a supportive method for predicting the bitterness of hydrolysates. However, this statement needs to be confirmed experimentally.

Keywords

• bioinformatics
• BIOPEP-UWM database
• bitter-tasting peptides
• hydrolysates
• soybean proteins