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ISSN: 2155-6199

Journal of Bioremediation & Biodegradation
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Research Article

Production, Partial Purification and Characterization of an Extracellular Psychrotrophic Lipase from Pseudomonas Sp. ADT3

Arpita Dey1,4*, Amarnath Chattopadhyay2, Subhra Kanti Mukhopadhyay2, Pradipta Saha2, Sabyasachi Chatterjee1, Tushar Kanti Maiti3 and Pranab Roy4
1Department of Biotechnology, The University of Burdwan, India
2Department of Microbiology, The University of Burdwan, India
3Department of Botany, The University of Burdwan, India
4Department of Biotechnology, Haldia Institute of Technology, India
Corresponding Author : Arpita Dey
Department of Biotechnology
The University of Burdwan, India
Tel: 0342 263 4975
E-mail: [email protected]
Received July 22, 2014; Accepted August 28, 2014; Published August 30, 2014
Citation: Dey A, Chattopadhyay A, Mukhopadhyay SK, Saha P, Chatterjee S, et al. (2014) Production, Partial Purification and Characterization of an Extracellular Psychrotrophic Lipase from Pseudomonas Sp. ADT3. J Bioremed Biodeg 5:242. doi:10.4172/2155-6199.1000242
Copyright: © 2014 Dey A, et al. This is an open-a ccess article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
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Abstract

Psychrotrophic Pseudomonas ADT3 (NCBI GenBank Acc.no.JX914667) is capable of growth on lipid as the sole carbon source. In this paper, we report the purification and characterization of an extracellular lipase from psychrotroph, isolated from soil sample of Ny- Alesund, Svalbard, Arctic region. The Pseudomonas ADT3 isolate produces lipase enzyme in the extracellular minimal media with only 1% olive oil. The lipase was purified from the concentrated culture supernatant. The crude enzyme was partially purified by saturated ammonium sulphate precipitation followed by extensive dialysis. Enzyme activity was found to be induced 6-folds in presence of 1.2 mM lead ion but strongly inhibited by heavy metals Hg2+ as well as EDTA and β-mercaptoethanol. The purified lipase has activity at two pH optima of pH i.e. pH 3.5 and 8.5. Optimum temperature for lipase activity was recorded at 22cC. The purified active fraction of lipase exhibits specific activity of 527.8 U/mg. The Vmax and Km was 144.93 U/mg/min and 0.260 mM respectively determined using Lineweaver-Burk plot. Zymogram analysis revealed prominent lipase band at 13.9 kDa range in the 80% saturated ammonium sulphate purified enzyme fraction.

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