Biotransformation of glycidol by the unspecific wax ester synthase/acyl-CoA:diacylglycerol acyltransferase of Acinetobacter baylyi ADP1

Ok Bin Kim, Heinrich Luftmann, Alexander Steinbüchel

Research output: Contribution to journalArticlepeer-review

2 Scopus citations

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 languageEnglish
Pages (from-to)972-978
Number of pages7
JournalEuropean Journal of Lipid Science and Technology
Volume111
Issue number10
DOIs
StatePublished - Oct 2009

Keywords

  • Acyl-CoA:Diacylglycerol acyltransferase (WS/DGAT)
  • Biorefinery
  • Glycidol
  • Glycidyl acyl ester
  • Unspecific wax ester synthase

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