Functional properties of whey proteins as affected by dynamic high-pressure treatment

Abstract

An ultra high-pressure homogenizer was used to treat whey protein isolate solutions (3%, w/w). The treated solutions (up to 300 MPa) were characterised for both physico-chemical properties (particle size distribution, surface hydrophobicity and structural conformation) and functional properties (solubility, foaming stability and interfacial rheology). Dynamic high-pressure treatment did not affect the conformation of the proteins (determined by micro-calorimetry, size-exclusion chromatography and electrophoretic technique). This treatment dissociated large protein aggregates leading to unmasking of the buried hydrophobic groups without affecting protein solubility. Interactions may then occur between these groups that enhance the viscoelasticity of air-water interfaces (assessed by drop tensiometry) and improve foam stability (evaluated by sparging method). Dynamic high-pressure-treated whey proteins showed better foaming and stabilising properties.