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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Abstract-Lipases was produced by

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The most conserved regions for 15 hepatitis B virus complete genome of different subtypes were aligned using PCGENE software CLUSTAL to design a new pair of primer that can bind to each subtype of hepatitis B virus (HBV), to amplify PreS region of HBV genome. A pair of primer from these conserved patches was selected using software PRIMER and named as Nhepf1 and Nhepr1. Nhepf1, forward primer bound 2362-2385 nucleotides and Nhepr1, reverse primer bound 260-283 nucleotide amplify 1.12 Kb region of HBV genome that contain PreS sequence. The pair of primer was optimized for PCR. Nhepf1 and Nhepr1 annealed well at 50°C to subtype adw2 (American), adr4 (Japanese) and Pakistanian patient derived HBV DNA without any nonspecific bands. The results were found to be highly reproducible with greater accuracy.