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• W182018645 abstract "Lipolytic bacterium was screened from five pure bacteria cultures available in Enzymeand Microbial Technology laboratory in UPM. The stock cultures were tested for lipaseproduction. Two isolates (S5 and 205W) showed the highest activity in tripticase soybroth and brain heart infusions. These isolates were further incubated in different basalmedia. Isolate S5 was shown to give higher activity (0.327 Ulml) than isolate 205W inmedia MI and stable in various organic solvents tested. Therefore isolate S5 was chosenfor further studies. Based on its morphological, biochemical characteristics and 16srDNA sequence, strain S5 was identified as Pseudomonas aeruginosa. P. aeruginosalipase exhibited the highest relative activity with n-hexane (410%) for 20 min reaction.Optimum lipase production was obtained at pH 7.0 and 37°C at static condition withpeptone as the best nitrogen source and olive oil as the best carbon source. The bestinoculum size was 6%. The surfactants, Tween 60 and Tween 80 were found to enhancefor bacterial growth and lipase production by S5.The lipase was purified to homogeneity by affinity column chromatography and anionexchange column chromatography. The purified lipase was highly homogeneous asdetermined by sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDSPAGE)and the molecular mass was estimated to be 60 kDa by SDS-PAGE and G-100gel filtration column chromatography. The optimum temperature and pH of the purifiedenzyme was 45°C and pH 9.0, respectively. S5 lipase was stable at pH 6-9 for 30 min.The half-life of the S5 lipase at 45°C and 50°C was 2 h and 1 h, respectively. The lipaseexhibited high stability in the presence of n-dodecane, 1-pentanol and toluene. As formetal ions, it was found that ca2+ stimulated lipase activity in 15 min incubation time,while EDTA had no effect on lipase activity. However, the S5 lipase was stronglyinhibited by the addition of 1 mM phenyl methyl sulfonyl fluoride (PMSF) (87%inhibition) and 1 rnM of Pepstatin (76% inhibition) after 30 min incubation. The S5lipase exhibited the highest activity in the presence of palm oil as a substrate andfollowed by coconut oil. S5 lipase was found to have the highest activity against trioleinwhich possess longer carbon chain length. S5 lipase is a non-specific lipase as shown bytriolein hydrolysis.The gene encoding for the intracellular lipase of P. aeruginosa strain S5 was isolated viagenomic DNA library and cloned into pRSET. The cloned sequence included two openreading frames (OW) consisting of 1575 bp for the first ORF (ORF1) and 582 bp forthe second ORF (ORF2). The OW2 was located at the downstream and function as theact gene for O w l . The conserved pentapeptide Gly- X- Ser- X-Gly was located in theORF1. Catalytic triad resembling of that serine protease, consisting of serine, histidine,aspartic acid or glutarnic acid residues was present in this lipase gene. Expression inE.coli resulted a 100-fold increase in enzyme activity after 9 h induction with 0.75 mMIPTG. The recombinant plasmid revealed a size of 60 kDa on SDS-PAGE. The Lip S5gene was stable in the presence of 25% (v/v) n-dodecane and n-tetradecane after 2 hincubation at 37OC. Predicted 3D structure of S5 lipase revealed topological organizationof a / @-hydrolase fold consisting of 10 a-Helices and 5 @-strands. The Ramachandranplot of S5 lipase showed that 85.8% (229) of residues lie in the most-favored region andonly 2.2% (6) of residue lie in generously allowed regions and 1 residue lie indisallowed region." @default.
• W182018645 created "2016-06-24" @default.
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• W182018645 date "2005-11-01" @default.
• W182018645 modified "2023-09-24" @default.
• W182018645 title "Production, Characterization And Expression Of An Organic Solvent Tolerant Lipase From Pseudomonas Aeruginosa S5s5" @default.
• W182018645 hasPublicationYear "2005" @default.
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