The purpose of this research was to better understand the mechanisms by which proteins affect the rates of lipid oxidation in order to develop protein-stabilized emulsion delivery systems with maximal oxidative stability. This study evaluated the affect of pH and emulsifier concentration on the stability of cumene hydroperoxide in hexadecane-in-water emulsions stabilized by β-lactoglobulin (β-Lg). Emulsions prepared with 0.2 wt % β-Lg (at pH 7.0) showed a 26.9% decrease in hydroperoxide concentrations 5 min after 0.25 mM ferrous ion was added to the emulsion. EDTA, but not continuous phase β-Lg, could inhibit iron-promoted lipid hydroperoxide decomposition. Lipid hydroperoxides were more stable to iron-promoted degradation at pH values below the pI of β-Lg, where the emulsion droplet would be cationic and thus able to repel iron away from the lipid hydroperoxides. Heating the β-Lg-stabilized emulsions to produce a cohesive protein layer on the emulsion droplet surface did not alter the ability of iron to decompose lipid hydroperoxides. These results suggest that proteins at the interface of emulsion droplets primarily stabilize lipid hydroperoxides by electrostatically inhibiting iron−hydroperoxide interactions.