Title of article
Optimisation of expression and immobilized metal ion affinity chromatographic purification of recombinant (His)6-tagged cytochrome P450 hydroperoxide lyase in Escherichia coli
Author/Authors
Delcarte، نويسنده , , Jérôme and Fauconnier، نويسنده , , Marie-Laure and Jacques، نويسنده , , Philippe and Matsui، نويسنده , , Kenji and Thonart، نويسنده , , Philippe and Marlier، نويسنده , , Michel، نويسنده ,
Issue Information
روزنامه با شماره پیاپی سال 2003
Pages
8
From page
229
To page
236
Abstract
Fatty acid hydroperoxide lyase (HPL) is a cytochrome P450 acting on fatty acid’s hydroperoxides in many plants. The optimisation of the expression of recombinant (His)6-tagged HPL in Escherichia coli is described: the highest HPL production yield were obtained with TB medium supplemented with 2.5 mM δ-aminolevulinic acid and 0.5 mM IPTG. For the first time, the time course expression of a plant P450 in a bench-scale fermentor is detailed and the amount of recombinant HPL production is 16.3 mg/l. The UV–Visible spectrum of the recombinant (His)6-tagged HPL have been recorded after a Ni2+-based affinity chromatography (IMAC).
Keywords
Histidine tag , Hydroperoxide lyase , cytochrome P450
Journal title
Journal of Chromatography B
Serial Year
2003
Journal title
Journal of Chromatography B
Record number
1454988
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