An extracellular lipase produced by marine fish intestinal isolate Halobacillus sp. AP-MSU 8 was purified and characterized. The lipase was purified to homogeneity using ammonium sulphate precipitation, DEAE-Sepharose anion exchange chromatography and Sephadex G-75 gel filtration chromatography. The overall purification protocols resulted in 25 % yield of lipase with 10.6-fold. The SDS-PAGE (12 %) analysis of purified lipase resulted in the molecular mass of the purified lipase as 25-kDa. The optimum pH and temperature required for maximum activity of purified lipase was 9.0 and 40°C respectively. Also, this lipase is halo tolerant and requires 2.5 M NaCl for maximum activity. The activity of the purified lipase was more in the presence of BaCl 2 and MgSO 4 , and in contrast the enzyme activity was totally inhibited in the presence of ZnSO 4 and ZnCl 2 . The surfactants such as polyethylene glycol and Tween 20 enhanced the lipase activity. Likewise 10 % concentration of organic solvents such as benzene and acetone stimulated the lipase activity, whereas at 20 % concentration all the tested solvents inhibited the lipase activity.