ISSN: 0973-7510

E-ISSN: 2581-690X

Baljot Kaur1, Monica Sachdeva Taggar2 , Poonam Sharma3 and Manjeet Kaur Sangha1
1Department of Biochemistry, Punjab Agricultural University, Ludhiana – 141004, India.
2School of Energy Studies for Agriculture, Punjab Agricultural University, Ludhiana – 141004, India.
3Department of Plant Breeding and Genetics, Punjab Agricultural University, Ludhiana – 141004, India
J. Pure Appl. Microbiol., 2016, 10 (2): 1435-1442
© The Author(s). 2016
Received: 03/02/2016 | Accepted: 09/03/2016 | Published: 30/06/2016

An extracellular lipase produced by Pseudomonas aeruginosa KF 853103 was purified to 15-fold with a specific activity of 1671.9 pkat mg-1 protein after ammonium sulphate precipitation and DEAE-cellulose column chromatography. The purified enzyme showed pH optima of 8.0 and temperature 40°C and was relatively stable within the temperature range of 30-40°C. The enzyme retained 96.5, 80.3 and 93.4 of its maximum activity in the presence of methanol, ethanol and acetone, respectively. However, the relative activity of enzyme was comparatively less in the presence of hexane and propanol (64.8 and 52.8%). The Km and Vmax values for lipase were found to be 0.136mM and 71.4 pkat ml-1, respectively. From the study of effect of temperature on Km and Vmax, free energy change (ΔG), enthalpy change (ΔH), entropy change (ΔS) and energy of activation (Ea) were reported to be -23.2 kJ mol-1, 15.9 kJ mol-1, 124.7 J K-1 mol-1 and 19.1 kJ mol-1, respectively.


Extracellular lipase, Pseudomonas aeruginosa, Purification.

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© The Author(s) 2016. Open Access. This article is distributed under the terms of the Creative Commons Attribution 4.0 International License which permits unrestricted use, sharing, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made.