Inhibition of Lipid Oxidation in Oil-in-Water Emulsions by Interface-Adsorbed Myofibrillar Protein.

This study investigated the role of interfacial myofibrillar protein (MFP) in the oxidative stabilization of meat emulsions. Emulsions with 10% oil were prepared using either 2% (w/v) Tween 20 or 0.25, 0.5, and 1% (w/v) MFP and then subjected to hydroxyl radical oxidation at 4 °C for 0, 2, and 24 h. MFP was more readily oxidized (intrinsic fluorescence quenching, sulfur losses, and carbonyl formation) than oil [conjugated dienes and 2-thiobarbituric acid-reactive substances (TBARS)]. However, oxidized MFP in the continuous phase stimulated lipid oxidation after 24 h, sharply contrasting with interface-adsorbed MFP that inhibited TBARS formation nearly 90% (p < 0.05). Interfacial MFP from 2 h oxidized samples exhibited greater losses of fluorescence and more extensive polymerization of myosin (detected by sodium dodecyl sulfate-polyacrylamide gel electrophoresis) than MFP present in the continuous phase. Results indicated that, due to the physical localization, interface-adsorbed MFP in general and myosin in particular provided accentuated protection of emulsions against oxidation.