Abstract
Lipid oxidation often occurs during egg white protein (EWP) storage and processing periods. Here, 2,2′-azobis (2-amidinopropane) dihydrochloride (AAPH) was performed to simulate lipid oxidation to probe the oxidation effects on foaming and structural properties of EWP. Results indicated that EWP structure became unfolding and flexible after oxidation, resulting in more hydrophobic groups and negative charge exposed and soluble aggregates formed, which revealed by the results of DLS and AFM. Additionally, high resolution mass spectrometry results evidenced that ovotransferrin and lysozyme trended to be new oxidation targets with the AAPH concentration increasing, and the oxidation sites inside lysozyme proved that EWP unfolding and exposure of internal hydrophobic amino acids, which were related to the enhancement of EWP foaming properties. Overall, our study provided a further analysis of the lipid induced oxidation of EWP, which may contribute to provide a more accurate strategy for enhancing protein foaming properties in food industry.
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