The sonication-induced changes in the structural and thermal properties of proteins in reconstituted whey protein concentrate (WPC) solutions were examined. Differential scanning calorimetry, UV-vis, fluorescence and circular dichroism spectroscopic techniques were used to determine the thermal properties of proteins, measure thiol groups and monitor changes to protein hydrophobicity and secondary structure, respectively. The enthalpy of denaturation decreased when WPC solutions were sonicated for up to 5 min. Prolonged sonication increased the enthalpy of denaturation due to protein aggregation. Sonication did not alter the thiol content but resulted in minor changes to the secondary structure and hydrophobicity of the protein. Overall, the sonication process had little effect on the structure of proteins in WPC solutions which is critical to preserving functional properties during the ultrasonic processing of whey protein based dairy products.

In recent years, the physical and chemical effects of ultrasound in liquid and solid media have been extensively used in food processing applications. Harnessing the physical forces generated by ultrasound, in the absence and presence of cavitation, for specific food processing applications such as emulsification, filtration, tenderisation and functionality modification have been highlighted. While some applications, such as filtration and emulsification are "mature" industrial processes, other applications, such as functionality modification, are still in their early stages of development. However, various investigations discussed suggest that ultrasonic processing of food and dairy ingredients is a potential and viable technology that will be used by many food industries in the near future.

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Compositional differences of acid whey (AW) in comparison with other whey types limit its processability and application of conventional membrane processing. Hence, the present study aimed to identify chemical and physical properties of AW solutions as a function of pH (3 to 10.5) at 4 different temperatures (15, 25, 40, or 90°C) to propose appropriate membrane-processing conditions for efficient use of AW streams. The concentration of minerals, mainly calcium and phosphate, and proteins in centrifuged supernatants was significantly lowered with increase in either pH or temperature. Lactic acid content decreased with pH decline and rose at higher temperatures. Calcium appeared to form complexes with phosphates and lactates mainly, which in turn may have induced molecular attractions with the proteins. An increase in pH led to more soluble protein aggregates with large particle sizes. Surface hydrophobicity of these particles increased significantly with temperature up to 40°C and decreased with further heating to 90°C. Surface charge was clearly pH dependent. High lactic acid concentrations appeared to hinder protein aggregation by hydrophobic interactions and may also indirectly influence protein denaturation. Processing conditions such as pH and temperature need to be optimized to manipulate composition, state, and surface characteristics of components of AW systems to achieve an efficient separation and concentration of lactic acid and lactose.