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Characterization of an extracellular alkaline lipase from Pseudomonas mendocina M-37

✍ Scribed by Praveen Dahiya; Pooja Arora; Ashok Chaudhury; Subhash Chand; Neeraj Dilbaghi

Publisher
John Wiley and Sons
Year
2010
Tongue
English
Weight
274 KB
Volume
50
Category
Article
ISSN
0233-111X

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✦ Synopsis

Abstract

A strain of Pseudomonas mendocina producing extracellular lipase was isolated from soil. The bacterium accumulates lipase in culture fluid when grown aerobically at 30 °C for 24 h in a medium composed of olive oil (1%) as substrate. Pseudomonas mendocina lipase was optimally active at pH 9.0, temperature of 50 °C and was found to be stable between pH 7.0–11.0. The lipase was inhibited by detergents such as SDS and Tween‐80. The enzyme was stable in various organic solvents tested with maximum stability in chloroform followed by toluene and exhibited 1–3 regiospecificity for hydrolytic reaction. This lipase was capable of hydrolyzing a variety of lipidic substrates and is mainly active towards synthetic triglycerides and fatty acid esters that possess a butyryl group. Metal ions like Mg^2+^, Ca^2+^ and Na^+^ stimulated lipase activity, whereas, Cu^2+^, Mn^2+^ and Hg^2+^ ions caused inhibition. (© 2010 WILEY‐VCH Verlag GmbH & Co. KGaA, Weinheim)

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