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This study aimed to investigate the relative reaction rate of protein and lipid oxidation in different biphasic model systems (linoleic acid; liposome; emulsion) containing myofibrillar protein (MFP at 1, 8 and 20 mg/mL) under hydroxyl radical stress. Protein oxidation markers exhibited significant changes in 2 h: reduced tryptophan fluorescence intensity, carbonyl formation, and extensive polymerization of myosin. In contrast, no detectable changes ( P  > .05) in lipid peroxide occurred within 2 h except for samples with 1 mg/mL MFP which showed an early TBARS formation. Of the three biphasic systems, the oxidative stability of lipids followed the order of emulsion > linoleic acid > liposome, indicating the steric role of proteins. In general, MFP was more susceptible to radicals than lipids, and a higher protein:lipid ratio was associated with a slower TBARS production and more rapid protein oxidation, suggesting a sacrificing role of MFP to protect lipids. [ABSTRACT FROM AUTHOR]