Influence of low-frequency ultrasound on the physico-chemical and structural characteristics of milk systems with varying casein to whey protein ratios

Casein and whey proteins respond differently to ultrasound treatment depending on the individual protein fraction and the delivered energy density. The main aim of this study was to determine the sonication-induced physiochemical and structural changes of protein solutions with varying casein to whey protein ratios as a function of processing time at 20 kHz ultrasound. Four different casein:whey protein ratios (80:20, 60:40, 50:50, 40:60) were prepared. Upon sonication, there was a reduction in particle size of the 80:20 and 60:40 ratios, but the particle size of 50:50 and 40:60 increased. Milk protein solutions with higher portion of caseins produced more hydrophobically driven aggregates while whey protein-rich milk protein solutions produced more disulphide mediated aggregates during sonication. Primarily, β-lactoglobulin was involved in the hydrophobic aggregation process and β-lactoglobulin, bovine serum albumin and κ-casein participated in the disulphide aggregation process at all ratios.