Abstract
In this work, we developed a novel approach combining bioinformatics, testing of functionality and bottom-up proteomics to obtain peptide emulsifiers from potato side-streams. This is a significant advancement in the process to obtain emulsifier peptides and it is applicable to any type of protein. Our results indicated that structure at the interface is the major determining factor of the emulsifying activity of peptide emulsifiers. Fish oil-in-water emulsions with high physical stability were stabilized with peptides to be predicted to have facial amphiphilicity: (i) peptides with predominantly α-helix conformation at the interface and having 18–29 amino acids, and (ii) peptides with predominantly β-strand conformation at the interface and having 13–15 amino acids. In addition, high physically stable emulsions were obtained with peptides that were predicted to have axial hydrophobic/hydrophilic regions. Peptides containing the sequence FCLKVGV showed high in vitro antioxidant activity and led to emulsions with high oxidative stability. Peptide-level proteomics data and sequence analysis revealed the feasibility to obtain the potent emulsifier peptides found in this study (e.g. γ-1) by trypsin-based hydrolysis of different side streams in the potato industry.
Highlights
In this work, we developed a novel approach combining bioinformatics, testing of functionality and bottom-up proteomics to obtain peptide emulsifiers from potato side-streams
The facial amphiphilicity of α-helix or β-strand structures (Fig. 1a,b) implies that the peptides can anchor at the interface with its hydrophobic face projected into the non-polar oil-phase and the hydrophilic face projected into the polar aqueous-phase[32,50]
We demonstrated the potential of a novel combination of bioinformatics prediction, functionality testing and bottom-up proteomics to identify peptide emulsifiers embedded in potato proteins
Summary
We developed a novel approach combining bioinformatics, testing of functionality and bottom-up proteomics to obtain peptide emulsifiers from potato side-streams. Emulsifiers have an influence on the chemical stability of emulsions (e.g. oxidative stability) by determining the properties of the oil-water interface (i.e., thickness, porosity, charge, antioxidant activity). These interfacial properties play a critical role on the interaction between oil and prooxidants such as radicals, oxygen and trace metals[5]. It is worth mentioning that the approach suggested in this work can be applied to any other protein-based raw material, including other types of protein-rich side-streams derived from the food and feed industry
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