The Delta 5-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 Delta 5-desaturase, at 20-22 degrees C and 20% oxygen, is surprisingly high yielding 22% of C16:1,Delta 5 (5-cis-palmitoleic acid) and 13% C18:2,Delta 5 Delta 11 (efedrenic acid). Lower amounts of other mono- and doubly-Delta 5-unsaturated fatty acids were also detected. These findings demonstrate that Delta 5-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 Delta 5 unsaturated fatty acid derivatives.
The desaturase from Bacillus subtilis a promising tool for the selective olefination of phospholipids.
Colotti G;Boffi A
2006
Abstract
The Delta 5-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 Delta 5-desaturase, at 20-22 degrees C and 20% oxygen, is surprisingly high yielding 22% of C16:1,Delta 5 (5-cis-palmitoleic acid) and 13% C18:2,Delta 5 Delta 11 (efedrenic acid). Lower amounts of other mono- and doubly-Delta 5-unsaturated fatty acids were also detected. These findings demonstrate that Delta 5-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 Delta 5 unsaturated fatty acid derivatives.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
