Isolation, Optimisation and Purification of Lipase Production by Pseudomonas Aeruginosa | OMICS International | Abstract
ISSN: 2155-952X

Journal of Biotechnology & Biomaterials
Open Access

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Research Article

Isolation, Optimisation and Purification of Lipase Production by Pseudomonas Aeruginosa

Benattouche Zouaoui1* and Abbouni Bouziane2

1Department of biology, Faculty of Science, Mascara University, Algeria

2Department of biology, Faculty of Science, Sidi belabbes University, Algeria

Corresponding Author:
Benattouche Zouaoui
Department of biology, Faculty of Science
Mascara University, Algeria
Tel: 00213 557172691
Fax: 0021348646312
E-mail: [email protected]

Received date: November 10, 2011; Accepted date: December 19, 2011; Published date: December 21, 2011

Citation: Zouaoui B, Bouziane A (2011) Isolation, Optimisation and Purification of Lipase Production by Pseudomonas Aeruginosa. J Biotechnol Biomaterial 1:120. doi:10.4172/2155-952X.1000120

Copyright: © 2011 Zouaoui B, et al. This is an open-access 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.


Six isolates of lipase producing (Ps1, Ps2, Ps3, Ps4, Ps5 and Ps6) were secreened from wastewater on a selective medium agar that contained tween 80 or olive oil as the only source of carbon. The isolate showed highest lipase activity was Ps5 which later was identified as Pseudomonas aeruginosa. The effect of media composition was analysed to maximize production of lipase. The maximum extracellular lipase present in the broth was purified 11 folds with an overall yield of 65.51 % through purification procedure of ammonium sulphate precipitation and DEAE cellulose chromatography. The purified lipase had maximal activity within the pH range of 6-8, with an optimum PH of 7, and within the temperature range of 25 – 35°C, with optimum temperature for the hydrolysis of olive oil at 35°C. The lipase activity of the enzyme was enchanced by Ca+2 and Mg+2 but strongly inhibited by heavy metals Zn+2, Cu+2and Mn+2.