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Hindi 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: arpitadey086@gmail.com |
| 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.
