Targeted hydrolysis of native potato protein: A novel workflow for obtaining hydrolysates with improved interfacial properties

Peptides and protein hydrolysates are promising alternatives to substitute chemical additives as functional food ingredients. In this study, we present a novel workflow for producing potato hydrolysate with improved emulsifying foaming properties using quantitative proteomics bioinformatic prediction facilitate targeted hydrolysis design. Based on previous studies, selected 15 potent emulsifier peptides derived from abundant proteins targets. Through in silico analysis, determined that range of industrial proteases (Neutrase (Neut), Alcalase (Alc), Flavourzyme (Flav) Trypsin (Tryp)), Tryp was found more likely release resembling the After applying all individually, were assayed vitro properties. No direct correlation between degree interfacial found. (E/S = 3%) produced (DH 5.4%) high aqueous solubility highest (P < 0.05) abilities, validating hypothesis. Using LC-MS/MS, identified >10,000 each hydrolysate. Peptide mapping revealed random overlapping known peptide emulsifiers is not sufficient quantitatively describe functionality. However, validated by 3% appears increase surface activity Our data also suggest terminal hydrophobic anchor domains may be important partitioning activity. While modest yields residual unhydrolyzed indicate room process improvement, work shows bioinformatics-guided data-driven promising, interdisciplinary approach design production alternative sources.