This study involves purification of a wild low-temperature lipase from a strain of Bacillus phychrophilus and analysis of its enzymatic characters. Electrophoretic pure enzyme on the SDS-PAGE was obtained through ammonium sulfate precipitation, phenyl superpose hydrophobic chromatography and Q FF anion-exchange chromatography.The optimum temperature of the enzyme is 25℃, which still has 25% relative lipase activity at 0℃. The activity of the lipase almost completely lost after incubation at 60℃ for 30 min. Lipase activity is independent of divalent cation. And the structure of this lipase may contain disulfide bond. The K_m and V_max of lipase under pH8.0 and 25℃ were 2.65×10^-5mol/L and 5.21mmol/(L·min) respectively.