Characterization and kinetics of whey protein isolate amyloid fibril aggregates under moderate electric fields.

Food proteins solutions enable the controlled flow of electrical current when subjected to a Moderate electric field (MEF). This application results in internal heat generation, known as ohmic heating, accompanied by electrochemical reactions. These effects play a significant role in influencing the formation of protein amyloid fibril aggregates (AFA), which have broad applications in food and biomedical fields, ranging from improving food texture to biomedical applications such as drug delivery and disease treatment. This study focused on investigating the formation of β-Lactoglobulin (β-lg) AFA under MEF conditions using WPI as protein source and various characterization techniques (e.g., Thioflavin T fluorescence, circular dichroism, and electron microscopy). The results indicated that MEF prolonged the lag phase of AFA formation. Furthermore, nucleation and fibril growth showed higher activation coefficients and cooperativity level (n > 2) compared to conventional heating method. MEF treatment resulted in unique fibril clustering and the presence of unexpected higher-order AFA networks confirmed by electron microscopy. These findings highlight the significant role of MEF in influencing the aggregation kinetics of β-lg AFA. Exploring further into the electrochemical and thermal effects during protein aggregation processes holds the key to unlocking deeper insights into fibril formation process.