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Abstract: The properties of n-tetradecane emulsions with dipalmitoylphosphatidylcholine (DPPC) or dioleoylphosphatidylcholine (DOPC) in 1M ethanol were investigated at 20 and 37°C. The zwitterionic phospholipids having the same headgroup bound to the apolar tail composed of two saturated or unsaturated chains were used as stabilizing agents. Both phospholipids may self-organize into aggregates, which possess different sizes and surface affinities. Electrokinetic properties of the systems at natural pH or pH 8 were investigated taking into account the effective diameter of the droplets as well as the zeta potentials using the dynamic light scattering technique. The effect of both phospholipids decreases the initially negative zeta potential of the n-tetradecane emulsion and is more evident in the case of DPPC especially at a physiological temperature near its main temperature transition. The change of zeta potential by DOPC is visible at both temperatures probably as an effect of a loose packing of this phospholipid on n-tetradecane droplets, because of the presence of double bonds in its molecule. Also, the role of ethanol dipoles on the stability of oil/phospholipid emulsions is obvious. The other aim of paper was the characterization of the phospholipase A2 influence on DOPC hydrolysis in the emulsion environment in order to emphasize the importance of such methodology. The present work is the first study that explores the effects of both electrolyte ions and ethanol molecules on DOPC hydrolysis by phospholipase. The effect of enzyme on the n-tetradecane/DOPC emulsions was investigated at pH 8 with Na+ or Ca2+ ions, which occur in the physiological fluids. The effective diameters do not always correlate with the zeta potentials. A possible reason of such behavior might a mechanism different from the electrostatic stabilization. The particular role of Ca2+ ions in the emulsions with phospholipids was confirmed. Those investigations provide insight into the properties of the PLA2 hydrolysis process enhanced by added ethanol. It is believed that the enzyme effect on the phospholipid aggregation behavior at the oil–water interface will be helpful for understanding other biological phenomena. [Copyright &y& Elsevier]