The desaturase from Bacillus subtilis, a promising tool for the selective olefination of phospholipids.
The Delta5-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 Delta5-desaturase, at 20-22 degrees C and 20% oxygen, is surprisingly high yielding 22% of C16:1,Delta5 (5-cis-palmitoleic acid) and 13% C18:2, Delta5 Delta11 (efedrenic acid). Lower amounts of other mono- and doubly-Delta5-unsaturated fatty acids were also detected. These findings demonstrate that Delta5-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 Delta5 unsaturated fatty acid derivatives.
Bonamore
Alessandra
A
Department of Biochemical Sciences, University "La Sapienza", Piazza Aldo Moro 5, 00185 Rome, Italy.
Macone
Alberto
A
Colotti
Gianni
G
Matarese
Rosa Marina
RM
Boffi
Alberto
A
D001412:Bacillus subtilis / Q000201:enzymology* / Q000235:genetics; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics; D000090943:Delta-5 Fatty Acid Desaturase; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics; D044943:Fatty Acid Desaturases / Q000737:chemistry* / Q000235:genetics; D010084:Oxidation-Reduction; D010743:Phospholipids / Q000737:chemistry*; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics
D001426:Bacterial Proteins; D000090943:Delta-5 Fatty Acid Desaturase; D010743:Phospholipids; D011994:Recombinant Proteins; D044943:Fatty Acid Desaturases