The liquid-liquid extraction of lipase A from Candide cylindracea and lipase B from porcine pancrease was carried out using reversed micellar organic solvents. Effects of various factors such as ionic strength, pH, and species and concentration of surfactant, on lipase solubilization were studied. A cationic surfactant cetyl-trimethyl ammonium bromide (CTAB) in isooctane/nhexanol(1:1) was found to be an effective solvent and its optimum concentration was 50 mM. KCl among various salts tested was the most effective and the efficiency of solubilization of lipase increased with decreasing the ionic strength of salts. The maximum activity and solubiliz ation of protein were obtained at pH 8. The stripping efficiency has a maximum value at pH 4 and increases with KCl concentration in the range of 0.2∼1.0 M. After the solubilization and stripping, the overall recovery efficiency of mass and specific activity of lipases was 62% and 66%, respectively.