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Purification and characterization of an alkaline lipase from Pseudomonas aeruginosa isolated from putrid mineral cutting oil as component of metalworking fluid

Paper ID Volume ID Publish Year Pages File Format Full-Text
22136 43256 2006 8 PDF Available
Title
Purification and characterization of an alkaline lipase from Pseudomonas aeruginosa isolated from putrid mineral cutting oil as component of metalworking fluid
Abstract

Extracellular lipase was isolated and purified from the culture broth of Pseudomonas aeruginosa, an extremophile which naturally grows in water-soluble mineral cutting oil (pH 10) used as metalworking fluid (MWF) for cooling and lubrication in industrial metalworking processes. The molecular mass of the purified lipase was estimated by SDS–PAGE to be 54 kDa. The optimum pH and temperature were 11 and 70°C, respectively. The enzyme is stabile over a broad pH range (pH 4–11.5). The lipase preferably acted on triacylglycerols with medium-chain fatty acids. The lipase was inhibited strongly by Zn2+, Hg2+, Cu2+ and slightly by Ca2+ and Mg2+. Non-ionic detergents and sodiumdeoxycholate enhanced lipase activity. Alkaline lipase from P. aeruginosa, capable of growing in a water-restricted medium has excellent properties and good potential for biotechnological applications in the metal industry. Its marked stability and activity in organic solvents suggest that this lipase is highly suitable as a biotechnological tool in a water-restricted medium with a variety of applications including organosynthetic reactions and the control and prevention of MWF putrification in the metal industry.

Keywords
Pseudomonas aeruginosa; alkaline lipase; mineral cutting oil; metalworking fluid; water-restricted mediumDDS, drug delivery system; DFP, di-iso-propyl fluorophosphate; DTT, dithiothreitol; IAA, iodoacetamide; MWF, metalworking fluid; pNPP, p-nitrophenyl p
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Purification and characterization of an alkaline lipase from Pseudomonas aeruginosa isolated from putrid mineral cutting oil as component of metalworking fluid
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Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Bioscience and Bioengineering - Volume 102, Issue 2, August 2006, Pages 82–89
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
100% Money Back Guarantee
Full-text PDF Download
Online Support
Any Questions? feel free to contact us