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Indian Journal of Biotechnology (IJBT) >
IJBT Vol.04 [2005] >
IJBT Vol.04(2) [April 2005] >
| Title: | Lipase from Pseudomonas aeruginosa MTCC 2488: Partial purification, characterization and calcium dependent thermostability |
| Authors: | Kukreja, Vandana
Bera, M B |
| Keywords: | calcium dependent thermostability
lipase
lipase activity
P aeruginosa
Tween-20 |
| Issue Date: | Apr-2005 |
| Publisher: | CSIR |
| IPC Code: | Int. Cl.7 A01N63/02; C12N9/16, 9/20; C12R1: 385 |
| Abstract: | Psuedomonas 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. |
| Page(s): | 222-226 |
| ISSN: | 0975-0967 (Online); 0972-5849 (Print) |
| Source: | IJBT Vol.04(2) [April 2005]
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