Interfacial dilatational and emulsifying properties of ultrasound-treated pea protein

In this study, the structural, interfacial, and emulsifying properties of high-intensity ultrasound (HUS)-treated pea protein isolate (PPI_US) were investigated. HUS at 50% amplitude and 57-60 W·cm^-2 for 5 min markedly improved protein solubility (by 132%), surface hydrophobicity (by 173%), and reduced particle size (by 52%). These physicochemical changes in PPI_US led to more rapid protein adsorption at the oil-water interface, improved emulsifying activity (by 18-27%) and capacity (by 11%), and enhanced emulsion physical stability. The multilayer nature, albeit less elastic, of the interfacial membrane formed by PPI_US when compared to control protein (PPI_C), based on dilatational testing, contributed to the above results. Moreover, PPI_US-stabilized emulsions exhibited a tendency of being less susceptible to lipid oxidation during storage. Thus, structure-modifying HUS may be a valuable processing technology for the manufacture of pea protein-based emulsion foods.