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The desaturase from Bacillus subtilis, a promising tool for the selective olefination of phospholipids

Paper ID Volume ID Publish Year Pages File Format Full-Text
25791 43601 2006 5 PDF Available
Title
The desaturase from Bacillus subtilis, a promising tool for the selective olefination of phospholipids
Abstract

The Δ5-desaturase from Bacillus subtilis has been cloned in Escherichia coli BL21 cells and its enzyme activity has been investigated as a function of temperature and oxygenation by analyzing methyl ester adducts from the total lipid extract in GC–MS measurements. The present data bring out that the activity of recombinant Δ5-desaturase, at 20–22 °C and 20% oxygen, is surprisingly high yielding 22% of C16:1,Δ5 (5-cis-palmitoleic acid) and 13% C18:2,Δ5Δ11 (efedrenic acid). Lower amounts of other mono- and doubly-Δ5-unsaturated fatty acids were also detected. These findings demonstrate that Δ5-desaturase can accept a multiplicity of substrates and is endowed with an unprecedented activity among other acyl-lipid desaturases thus representing a unique tool for the production of rare Δ5 unsaturated fatty acid derivatives.

Keywords
Unsaturated fatty acids; Bacterial desaturases; Cyclopropane fatty acid synthase; Fatty acid methyl esters; Gas chromatography–mass spectrometry; Bacillus subtilis
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Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Biotechnology - Volume 121, Issue 1, 2 January 2006, Pages 49–53
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
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Price was $35.95
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