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Properties of a thermostable extracellular lipase from Bacillus megaterium AKG-1

โœ Scribed by Anurag Sekhon; Neetu Dahiya; Ram P. Tiwari; Gurinder S. Hoondal

Book ID
102389719
Publisher
John Wiley and Sons
Year
2005
Tongue
English
Weight
125 KB
Volume
45
Category
Article
ISSN
0233-111X

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โœฆ Synopsis

Abstract

An extracellular lipase isolated from Bacillus megaterium AKGโ€1 had an optimum activity at 55 ยฐC/pH 7.0. It retained 100% activity at 50 ยฐC for 30 min with a half life of 30 min at 70 ยฐC. A 20โ€“70% increase in lipase activity was observed in presence of acetone (20% v/v), DMSO (20% v/v) and isopropanol (10% v/v). The enzyme activity was 92, 98 and 107% after 24 h, on treatment with 10% (v/v) acetone, benzene and isopropanol respectively. Deoxycholic acid, sodium deoxycholate, lithocholic acid, rhamnolipid, Brij 52 and cholic acid stimulated the lipase activity by 76, 36, 24, 24, 23.6 and 13%, respectively. Addition of reducing agents like sodium sulphite, sodium metabisulphite and Lโ€cysteineโ€HCl, at 10 mM concentration stimulated lipase activity by 127, 146 and 150% respectively. The lipase appeared to show enantioselectivity in hydrolyzing racemic 3โ€acetoxyโ€ฮฒโ€lactam as it hydrolyzed only the (+) enantiomer. (ยฉ 2005 WILEYโ€VCH Verlag GmbH & Co. KGaA, Weinheim)

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