Lipase obtained from Streptomyces fungicidicus RPBS-A4 was partially purified using ammonium sulphate precipitation (80% w/v) followed by dialysis. Biochemical and physical properties of the purified enzyme was investigated and it showed molecular weight of 32.0 KDa and zymogram of yellowish band over a pink background. The purified enzyme was stable in the pH range of 8.0-11.0 and most lipase activity obtained at 12 hours of incubation in the pH value of 9.0. Thermo stability profile revealed that the enzyme showed 100% activity at 40°C and nearly 91.6% of the activity at 60°C. Lipase obtained was maximally stimulated by both the calcium and manganese ions. Among the organic solvents maximum activity was obtained in the presence of isoamyl alcohol followed by acetone. More than 63% of the enzyme activity was detected even in the existence of commercial detergents after 3 hours of incubation. The partially purified lipase removed the used motor oil spot more efficiently when coupled with detergents that were different than the detergents alone. Storage indicating that enzyme could be kept without a lot of reduction in its action for up to 20 days at room temperature.
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