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Purification and characterization of an extracellular lipase from a novel strain Penicillium sp DS-39 (DSM 23773)

Lookup NU author(s): Sanjay Antony-Babu

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Abstract

A newly isolated fungal strain, Penicillium sp. DS-39 (DSM 23773), was found to produce an inducible extracellular lipase when grown in a medium containing 1.0% (v/v) olive oil. Maximum lipase activity was obtained after 120h of incubation at 28 degrees C. The lipase was purified 129-fold with a final specific activity of 308.73 IU/mg. The molecular weight of the homogeneous lipase was 43 kDa as determined by SDS-PAGE. It was optimally active at pH 5.5 and 45 degrees C. The lipase was most active on triolein and exhibited a broad substrate range with a preference for triacylglycerols containing long chain unsaturated fatty acids. It showed no regio-specificity for the ester bond in triolein. It was activated by Ca2+ and Mn2+, while significant inhibition was observed with Hg2+ and Zn2+. The lipase showed significant stability and activation in the presence of organic solvents with log P >= 2.0. These features render Penicillium sp. DS-39 lipase (PEL) a potential biocatalyst for applications such as biodiesel production, enzymatic restructuring, by interesterification of different oils and fats, and biodegradation of oil spills in the environment. (C) 2011 Elsevier B.V. All rights reserved.

Publication metadata

Author(s): Dheeman DS, Antony-Babu S, Frias JM, Henehan GTM

Publication type: Article

Publication status: Published

Journal: Journal of Molecular Catalysis B: Enzymatic

Year: 2011

Volume: 72

Issue: 3-4

Pages: 256-262

Print publication date: 28/06/2011

ISSN (print): 1381-1177

ISSN (electronic): 1873-3158

Publisher: Elsevier BV

URL: http://dx.doi.org/10.1016/j.molcatb.2011.06.013

DOI: 10.1016/j.molcatb.2011.06.013

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