The Effect of Lipids on the Structure and Function of Egg Proteins in Response to Pasteurization

In recent years, the consumption of liquid eggs has failed to meet the expectations of the public due to growing concerns regarding food safety and health. It is well known that there are interactions between the components in liquid eggs, and the interaction effect on the structure and functional properties of the proteins and antigenicity remains unclear. To investigate egg component interactions, we focused on four major egg lipids, namely phosphatidylcholine, palmitic acid, oleic acid, and linoleic acid, as well as four major egg proteins, including ovalbumin, ovotransferrin, ovomucoid, and lysozyme. The protein structural changes were analyzed using polypropylene gel electrophoresis, circular dichroism, ultraviolet absorption spectra, and exogenous fluorescence spectra, and the functional properties were assessed through solubility measurements and particle size analysis, while protein antigenicity was evaluated using an enzyme-linked immunosorbent assay. All the results revealed that oleic acid had the most significant effect on proteins' secondary and tertiary structures, particularly affecting ovalbumin and ovotransferrin. Linoleic acid substantially increased the solubility of ovalbumin and ovomucoid, while palmitic acid significantly influenced the particle size of ovalbumin and lysozyme. Thus, we found that different lipids exhibit distinct effects on egg protein properties during pasteurization conditions, with oleic acid showing the most substantial impact on protein structure and antigenicity.