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Lipases catalyze the hydrolysis of long chain triglycerides. Microbial lipases are receiving much attention because of their industrial potential in the chemical, pharmaceutical, medical, cosmetic, biosurfactant synthesis, leather industries, mutation, agrochemicals and paper manufacturing industries. This article presents the isolation of maximum lipase producing bacteria and the optimization of different conditions for the maximum production of lipase. Bacillus subtilis PCSIRNL-39 shows maximum production of lipase at 45°C with pH 7 using nitrogen source peptone and carbon source sucrose. B. subtilis PCSIRNL-39 showed the best production at 5% inoculum size, while Ca 2+ and Mg 2+ were found best stimulator for enzyme production during the study. Tween 20 and 80 enhanced better lipase production than other surfactant. The kinetic parameters of V max and K m for the lipase were measured to be 101 µM/min.mL and 7.6 mg, respectively.

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In this study, the optimum growth conditions and lipolytic enzyme activity shown by the bacterial isolate (PCSIR NL-37) from the soil of Lahore (Punjab, Pakistan) are being reported. Lipolytic bacterial strains (100) isolated from soil and water samples from oil industry, mobile oil filling areas and kitchen wastages were screened on tributyrin agar and rhodamine agar plates. The strain PCSIR NL-37 was identified as Bacillus cereus following morphological, biochemical and molecular characterization. Best medium for lipase production was olive oil and mustard oil cake and the best carbon sources were fructose and maltose whereas yeast extract was found to be the best nitrogen source, showing 55U/mL enzyme activity. The best inoculum size for the growth of this strain was 4-5%. Optimum pH was 8 and best temperature was 40 o C for the reported strain. Addition of divalent Mg 2+ and Ca 2+ ions resulted in 2-fold increase in enzyme activity while SDS completely inhibit the lipase activity to zero.

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There is a growing trend to produce lipase from microorganisms owing to their commercial demand in various industries. Bacillus cereus has been shown to have extracellular lipase activity and high growth rates. This study explains the purification of microbial lipase to homogeneity by dialysis, precipitation and chromatography. The purified enzyme with 56kDa relative molecular mass exhibited the highest activity at 60°C (95.56U/ml) and pH 7 (124.50U/ml). The enzyme activity was highly promoted in the presence of K+ (136.17U/ml) and Zn++(133.07 U/ml), and SDS did not affect the enzyme activity, whereas in the company of triton X100 activity of lipase is maximum (23.90 U/ml). The enzyme activity was enhanced by using almond oil (120.00 U/ml) as a substrate. We deduce cheaper protocols for producing extracellular lipase via simple laboratory techniques, which could be a good insight for its production at the commercial level. Keywords: Lipase; Bacillus cereus; chromatography; enzyme activity; purification.