Lipid oxidation is a major cause for the degradation of biological systems and foods, but the intricate relationship between lipid oxidation and protein modifications in these complex multiphase systems remains unclear. The objective of this work was to have a spatial and temporal insight of the modifications undergone by the interfacial or the unadsorbed proteins in oil-in-water emulsions during lipid oxidation. Tryptophan fluorescence and oxygen uptake were monitored simultaneously during incubation in different conditions of protein-stabilized oil-in-water emulsions. Kinetic parameters demonstrated that protein modifications, highlighted by decrease of protein fluorescence, occurred as an early event in the sequence of the reactions. They concerned more specifically the proteins adsorbed at the oil/water interface. The reactions led in a latter stage to protein aggregation, carbonylation, and loss of protein solubility.

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