EFFECT OF THE OXIDATION OF FREE FATTY-ACIDS ON THE INTERFACIAL ADSORPTIVITY OF LYSOPHOSPHATIDYLCHOLINE FREE FATTY-ACID OVALBUMIN COMPLEXES

The effect of the oxidation of linoleic acid on the interfacial adsorptivity of lysophosphatidylcholine (LPC)/free fatty acid (FFA)/ovalbumin (OA) complexes was investigated by P-31-NMR. The interfacial adsorptivity of the complexes was evaluated by the mean droplet size, phosphorus signal and relaxation time of an emulsion composed of each complex. The interfacial adsorptivity of the LPC/FFA/OA complexes became lower with the oxidation of linoleic acid, which formed a complex with LPC and OA. Reduction of the T2 relaxation time and peak broadening of Ser-P68 for OA correlated well with the formation of tine emulsions from an LPC/linoleic acid/OA complex. The bilayer vesicles composed of LPC and linoleic acid with a low POV value were destroyed by coupling with protein and show high interfacial adsorptivity. On the other hand, the vesicles composed of LPC and linoleic acid with a high POV value remained in liposome and show low interfacial adsorptivity. These results suggest that the affinity of bilayer vesicles composed of LPC and FFA mainly promoted the interfacial adsorption of an LPC/FFA/OA complex, and that the region of Ser-P68 in OA was adsorbed at the interface when the complex formed a fine emulsion.