Reference : Optimisation Of Expression And Immobilized Metal Ion Affinity Chromatographic Purificati...

	Document type :	Scientific journals : Article
	Discipline(s) :	Life sciences : Microbiology
	To cite this reference:	http://hdl.handle.net/2268/4377

Title :	Optimisation Of Expression And Immobilized Metal Ion Affinity Chromatographic Purification Of Recombinant (His)(6)-Tagged Cytochrome P450 Hydroperoxide Lyase In Escherichia Coli
Language :	English
Author, co-author :	Delcarte, J. [ > > ]
	Fauconnier, Marie-Laure [Université de Liège - ULg > > Gembloux Agro-Bio Tech >]
	Jacques, P. [> > > >]
	Matsui, K. [> > > >]
	Thonart, Philippe [Université de Liège - ULg > > Gembloux Agro-Bio Tech - Biochimie et microbiologie industrielles >]
	Marlier, M. [ > > ]
Publication date :	2003
Journal title :	Journal of Chromatography B-Analytical Technologies In the Biomedicaland Life Sciences
Volume :	786
Issue/season :	1-2
Audience :	International
ISSN :	1570-0232
Keywords :	[en] expression ; Purification ; Escherichia coli ; Hydroperoxide lyase ; Cytochrome P450 ; Histidine tag
Abstract :	[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).
Permalink :	http://hdl.handle.net/2268/4377
DOI :	10.1016/S1570-0232(02)00815-2

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