Abstract
Glycidol was biologically derivatized by the unspecific wax ester synthase/acyl coenzyme A (acyl-CoA): diacylglycerol acyltransferase (WS/DGAT) from Acinetobacter baylyi ADP1 into glycidyl acyl ester. Catalysis of in vitro conversion of glycidol to glycidyl acyl ester by the WS/DGAT from A. baylyi was verified by (i) a radiometric assay, (ii) thin-layer chromatography and (iii) also by ESI-MS. A specific activity of 50 nmol·mg-1·min-1 was obtained when 10 mM glycidol and 5 μM palmitoyl-CoA were used. In vivo synthesized glycidyl acyl esters in recombinant E. coli were detected and quantified by staining with the epoxide-specific reagent 4-(4-nitrobenzyl)-pyridine. Of glycidyl acyl esters, 1.5 mg/L was obtained from the culture in the presence of 10 mM glycidol and 10 mM oleate.
Original language | English |
---|---|
Pages (from-to) | 972-978 |
Number of pages | 7 |
Journal | European Journal of Lipid Science and Technology |
Volume | 111 |
Issue number | 10 |
DOIs | |
State | Published - Oct 2009 |
Keywords
- Acyl-CoA:Diacylglycerol acyltransferase (WS/DGAT)
- Biorefinery
- Glycidol
- Glycidyl acyl ester
- Unspecific wax ester synthase