A comparative study on the effects of heat, ultrasound and high hydrostatic pressure on the structural and physicochemical properties of whey proteins

This study aimed to investigate the structural changes of whey protein isolate (WPI) caused by high intensity ultrasound (US), high hydrostatic pressure (HHP), and heat (HE), and their impact on important techno-functional properties such as solubility and isoelectric point. The results of FTIR spectroscopy revealed that HE and HHP increased β-sheets and unordered structures, while decreasing α-helices, resulting in a noticeable decrease in solubility and an increase in the isoelectric point. In contrast, US reduced intermolecular β-sheets and increased α-helices and random coils, leading to improved solubility. However, the effect of US on the isoelectric point was minimal. These structural changes were also reflected in the alteration of free amino and thiol groups, turbidity, particle size, and electrophoretic pattern. The findings of this study suggest that HE, US, and HHP can potentially be utilized to modify WPI structure to meet specific techno-functional requirements.

Abstract licence: CC BY-NC

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