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dc.contributor.authorKukreja, Vandana-
dc.contributor.authorBera, M B-
dc.identifier.issn0975-0967 (Online); 0972-5849 (Print)-
dc.description.abstractPsuedomonas aeruginosa MTCC 2488 produced lipase on Rhodamine B agar plates containing olive oil. Extra-cellular lipase activity was analyzed spectrophotometrically using Tween-20 as well as olive oil as substrate. The semipurified enzyme, precipitated by 30% saturated ammonium sulphate, showed 20.79 fold increase in specific activity (U/mg) and reduction in carbohydrate content to 1.7% as compared to the crude enzyme. The enzyme hydrolyzed Tween-20 and -40 better than Tween-60 and -80. Lipase has been found to be thermostable with maximum activity at 55-60oC but marked decrease was observed above this temperature. Ca2+ seemed to play an important role in the thermostability as 97% of enzyme activity was retained after 2 hr incubation at 65oC and 1hr incubation at 70oC in presence of 10 mM CaCl2. However, thermostability of the enzyme was decreased considerably in presence of 5 mM EDTA, confirming the enzyme to be a metalloprotein. Lipase has been found to be stable in presence of 30% acetone, methanol and ethanol. While, the enzyme activity was decreased by 30-50% in presence of n propanol, 2 propanol, n methyl propanol, isooctane and hexane. Further, 30% butanol resulted in ~65% decrease in the enzyme activity. Lipase has been found to be stable in presence of nonionic detergents, whereas anionic detergent, SDS completely inactivated the enzyme.en_US
dc.relation.ispartofseriesInt. Cl.7 A01N63/02; C12N9/16, 9/20; C12R1: 385en_US
dc.sourceIJBT Vol.4(2) [April 2005]en_US
dc.subjectcalcium dependent thermostabilityen_US
dc.subjectlipase activityen_US
dc.subjectP aeruginosaen_US
dc.titleLipase from Pseudomonas aeruginosa MTCC 2488: Partial purification, characterization and calcium dependent thermostabilityen_US
Appears in Collections:IJBT Vol.04(2) [April 2005]

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