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

摘要

Characterization of a Bacillus subtilis DELTA5-desaturase produced recombinantly in Escherichia coli BL21 is reported. Effects of temp. and O2 levels on enzyme activity were assessed by measuring methyl ester adducts in total lipid extracts. Max. enzyme activity was observed at 20-22degC and with 20% O2. Under these conditions, yields of 5-cis-palmitoleic acid and efedrenic acid were 22 and 13%, respectively, with lower levels of other single- and double-DELTA5-unsaturated fatty acids. It is concluded that the broad spectrum of activity of this DELTA5-desaturase, which is unusual amongst the acyl-lipid desaturases, makes it particularly suitable for the production of rare DELTA5 unsaturated fatty acid derivatives.