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

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.