Targeted hydrolysis of native potato protein: A novel workflow for obtaining hydrolysates with improved interfacial properties
Metadatos
Afficher la notice complèteEditorial
Elsevier
Materia
Potato protein Targeted hydrolysis Interfacial properties Quantitative proteomics Peptide identification
Date
2022-11-10Referencia bibliográfica
Simon Gregersen Echers... [et al.]. Targeted hydrolysis of native potato protein: A novel workflow for obtaining hydrolysates with improved interfacial properties, Food Hydrocolloids, Volume 137, 2023, 108299, ISSN 0268-005X, [https://doi.org/10.1016/j.foodhyd.2022.108299]
Patrocinador
Innovation Fund Denmark 7045-00021BRésumé
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 a potato protein hydrolysate with improved
emulsifying and foaming properties using quantitative proteomics and bioinformatic prediction to facilitate
targeted hydrolysis design. Based on previous studies, we selected 15 potent emulsifier peptides derived from
abundant potato proteins as targets. Through in silico analysis, we determined that from a range of industrial
proteases (Neutrase (Neut), Alcalase (Alc), Flavourzyme (Flav) and Trypsin (Tryp)), Tryp was found more likely
to release peptides resembling the targets. After applying all proteases individually, hydrolysates were assayed
for in vitro emulsifying and foaming properties. No direct correlation between degree of hydrolysis and interfacial
properties was found. Tryp (E/S = 3%) produced a hydrolysate (DH = 5.4%) with high aqueous solubility and
the highest (P < 0.05) emulsifying and foaming abilities, validating the hypothesis. Using LC-MS/MS, we
identified >10,000 peptides in each hydrolysate. Peptide mapping revealed that random overlapping with
known peptide emulsifiers is not sufficient to quantitatively describe hydrolysate functionality. However, validated
release of targeted peptides by 3% Tryp appears to increase surface activity of the hydrolysate. Our data
also suggest that terminal hydrophobic anchor domains may be important for high interfacial partitioning and
activity. While modest yields and residual unhydrolyzed protein indicate room for process improvement, this
work shows that bioinformatics-guided and data-driven targeted hydrolysis is a promising, interdisciplinary
approach to facilitate process design for production of functional hydrolysates from alternative protein sources.