Modification of whey protein concentrate hydrophobicity by high hydrostatic pressure

The functionality of protein molecules depends on hydrophobic, electrostatic, and steric parameters of the protein structure. Modifications of proteins that enhance hydrophobicity show promise for improving functional properties of foods. An increase in binding affinity or decrease in apparent dissociation constant indicates increased hydrophobicity. High hydrostatic pressure (HHP) affects the hydrophobicity of beta-lactoglobulin (β-LG), the primary protein in whey, and increases the binding affinity of β-LG for 1-anilino-naphthalene-8-sulfonate and cis-parinaric acid. However, little work has been done regarding the effects of HHP on whey protein concentrate (WPC) hydrophobicity and flavor-binding properties, and whether the presence of multiple proteins in WPC has significant influence on the behavior of whey proteins during HHP treatments. WPC is a good candidate for testing the practical utility of the application of HHP to modify the functional properties of a complex protein system since it is in the form that the ingredient is utilized in a number of food applications. The current work describes the effects of HHP on hydrophobicity of WPC and potential applications.