Reference : Optimisation Of Expression And Immobilized Metal Ion Affinity Chromatographic Purific...
Scientific journals : Article
Life sciences : Microbiology
http://hdl.handle.net/2268/4377
Optimisation Of Expression And Immobilized Metal Ion Affinity Chromatographic Purification Of Recombinant (His)(6)-Tagged Cytochrome P450 Hydroperoxide Lyase In Escherichia Coli
English
Delcarte, J. [> >]
Fauconnier, Marie-Laure mailto [Université de Liège - ULg > > Gembloux Agro-Bio Tech >]
Jacques, Philippe mailto [> > > >]
Matsui, K. [> > > >]
Thonart, Philippe mailto [Université de Liège - ULg > > Gembloux Agro-Bio Tech - Biochimie et microbiologie industrielles >]
Marlier, M. [> >]
2003
Journal of Chromatography B-Analytical Technologies In the Biomedicaland Life Sciences
786
1-2
Yes (verified by ORBi)
International
1570-0232
[en] expression ; Purification ; Escherichia coli ; Hydroperoxide lyase ; Cytochrome P450 ; Histidine tag
[en] 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) -tagged HPL in Escherichia coli is described: the highest HPL 6 production yield were obtained with TB medium supplemented with 2.5 mM d-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) -tagged HPL have been recorded after a Ni -based affinity chromatography (IMAC).
http://hdl.handle.net/2268/4377
10.1016/S1570-0232(02)00815-2

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