β-lactoglobulin (β-lg) is an important source of biologically and functionally active peptides that are of particular interest in agri-food, nutraceutical, and pharmaceutical industries. Enzymatic hydrolysis of proteins remains the most common mode of peptide production. However, efficient hydrolysis of proteins and particularly β-lg is difficult to perform due to their compact globular structure. Thus, the current study deals with green high-voltage electric treatments (HVET): pulsed electric fields and electric arc to pretreat β-lg and improve its proteolysis by trypsin and chymotrypsin. The results demonstrate substantial improvement of hydrolysis performance after the pretreatment of β-lg with HVET compared to the non-pretreated and preheated β-lg. Moreover, HVET led to the peptide release from β-lg even before the addition of proteases. Furthermore, pioneer studies of proteolysis kinetics and structural changes of β-lg molecules subjected to HVET allowed a better understanding of the mechanisms underlying hydrolysis improvement.

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Beta-lactoglobulin (β-lg) is a major whey protein with various techno-functional properties that can be improved by several treatments. Therefore, the objective of this study was to explore the impact of green high-voltage electrical treatments (HVETs)—namely, pulsed electric fields and electric arcs—on the functional properties of β-lg. Both emulsifying and foaming stability and capacity, as well as the hygroscopicity of non-treated and pretreated β-lg, were explored. The results demonstrated that the emulsifying capacity and stability of pretreated samples increased by 43% and 22% when compared to native β-lg, respectively. Likewise, the pretreated β-lg displayed better foaming stability compared to native β-lg. In addition, the HVETs significantly decreased the hygroscopicity of β-lg (by 48% on average), making it a good ingredient with reduced hygroscopicity for the food industry.