Recently, properties of thermostable lipases receive a very special interest as the enzymes are suited for harsh industrial processes. This research was aimed to purify a thermostable lipase produced by Bacillus licheniformis IBRL-CHS2 and to determine the properties that could give advantages to the industries. The enzyme was purified to 6.76-fold with 1.81% recovery by double steps of gel filtration chromatography. The molecular weight was shown to be 37.3 kDa. The purified lipase showed the maximum activity at 70^oC and pH 8.0. However, the lipase was more stable at 65^oC with the half-life of 29 hours. The activity was improved in the presence of Ca²⁺, K⁺, Zn²⁺, Mg²⁺, potassium iodide and 2-mercaptoethanol. Besides that, the activity also retained in all organic solvents tested. For the effect of surfactants, the activity was enhanced by Tween 20 and Span 40. The lipase showed highest activity towards olive oil and trimyristin (C_14:0) as compared to other substrates. The K_m value obtained was 0.60 mM and the V_max value was 101 mM
min^-1 when the substrate used was trimyristin. Properties showed by this lipase make it suitable for a wide range of application such as food industry, sewage treatment and organic synthesis.