In view of several biotechnological applications of microbial lipases, an attempt was made to characterize a lipase produced by Bacillus sp Lp5, a strain isolated from oil contaminated soil. Based on 16S rDNA analysis, it was identified as Bacillus strain Y IVI. In electrophoretic separation many bands were detec. The molecular weight of this protein was calculated to be about 35KD. The partially purified lipase of LP5 exhibited activity in a wide range of pH (4-10). Maximal activity (100%) was observed at pH 8.0. The relative activity was found to be 10.02%, 78.49%, 81.25%, and 8.18% at pH 4.0, 6.0, 10.0 and 12.0 respectively. This lipase retained 86.90% and 73.16% of its activity at 40⁰C and 80⁰C respectively.  The activity was found to be less at 20⁰C. The results revealed that a lipase activity of 124% and 109% was observed in presence of metal ions CaCl₂ and NaCl respectively. Inhibition of lipase by LP5 was detected with EDTA, ZnSO₄ , HgCl₂ and CuSO₄.The Enzyme activity  was 95.24%, 82.16%, 91.18%, and 62.15% with tributyrin, tween-20, tween-80, olive oil respectively. Inhibition of enzyme activity was observed when triton-x was employed as substrate.