References of "Fauconnier, Marie-Laure"
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See detailStudy of oxylipins during storage of potato flakes
Laine, G.; Goebel, C.; Feussner, I. et al

Conference (2005)

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See detailStimulation of the lipoxygenase pathway is associated with systemic resistance induced in bean by a nonpathogenic Pseudomonas strain
Ongena, MARC ULg; Duby, Franceline ULg; Rossignol, Fanny et al

in Molecular Plant-Microbe Interactions (2004), 17(9), 1009-1018

Systemic defense reactions induced in bean by the nonpathogenic Pseudomonas putida BTP1 strain reduced disease caused by Botrytis cinerea. Phenylalanine ammonialyase activity and the level of endogenous ... [more ▼]

Systemic defense reactions induced in bean by the nonpathogenic Pseudomonas putida BTP1 strain reduced disease caused by Botrytis cinerea. Phenylalanine ammonialyase activity and the level of endogenous free sallicylic acid were compared in plant growth-promoting rhizobacteria-treated versus control plants, but no significant differences were detected. Furthermore, no enhanced fungitoxicity was detected in methanolic leaf extracts, suggesting that accumulation of bean phytoalexins was not part of the stimulated defense mechanisms. However, BTP1-inoculated plants showed increased levels of both linoleic and linolenic acids. On this basis, we further investigated whether the lipoxygenase pathway, leading to antifungal phytooxylipins, could have been stimulated. Two key enzymatic activities of this metabolic route, namely lipoxygenase and hydroperoxidelyase, were significantly stimulated during the first four days after challenging BTP1-treated plants with the pathogen. This was observed in parallel with a more rapid consumption of the respective substrates of these enzymes, as revealed by measurements of endogenous concentrations of linolenic acid and their hydroperoxide derivatives. Moreover, headspace-gas chromatography analyses showed significantly higher concentrations of the fungitoxic final product Z-3-hexenal in leaves from BTP1-inoculated beans as compared with control plants. Taken together, these results strongly suggest that the oxylipin pathway can be associated with enhanced disease resistance induced in bean plants by nonpathogenic rhizobacteria. [less ▲]

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See detailLipid and oxylipin profile during storage of potato tubers
Fauconnier, Marie-Laure ULg; Welti, R.; Delaplace, Pierre ULg et al

Poster (2004, June 03)

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See detailLipid and oxylipin profile during storage of potato tubers
Fauconnier, Marie-Laure ULg; Welti, R.; Delaplace, Pierre ULg et al

Poster (2004, June 01)

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See detailLe stockage post-récolte : une étape clé du processus de production.
Delaplace, Pierre ULg; Fauconnier, Marie-Laure ULg

in Troupeaux et Cultures des Tropiques (2004), 4

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See detailValorisation industrielle de la pomme de terre.
Delaplace, Pierre ULg; Fauconnier, Marie-Laure ULg

in Troupeaux et Cultures des Tropiques (2004)

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See detailFormation Of Plant Cuticle: Evidence For The Occurrence Of The Peroxygenase Pathway
Lequeu, J.; Fauconnier, Marie-Laure ULg; Chammai, A. et al

in Plant Journal (2003), 36(2),

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See detailPotato Tuber Phospholipids Contain Colneleic Acid In The 2-Position
Fauconnier, Marie-Laure ULg; Williams, Td.; Marlier, M. et al

in FEBS Letters (2003), 538(1-3),

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See detailLipid And Oxylipin Profiles During Aging And Sprout Development In Potato Tubers (Solanum Tuberosum L.)
Fauconnier, Marie-Laure ULg; Welti, R.; Blee, E. et al

in Biochimica et Biophysica Acta-Molecular and Cell Biology of Lipids (2003), 1633(2),

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See detailOptimisation Of Expression And Immobilized Metal Ion Affinity Chromatographic Purification Of Recombinant (His)(6)-Tagged Cytochrome P450 Hydroperoxide Lyase In Escherichia Coli
Delcarte, J.; Fauconnier, Marie-Laure ULg; Jacques, P. et al

in Journal of Chromatography B-Analytical Technologies In the Biomedicaland Life Sciences (2003), 786(1-2),

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 ... [more ▼]

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). [less ▲]

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See detailFatty Acid Hydroperoxides Biotransformation By Potato Tuber Cell-Free Extracts
Fauconnier, Marie-Laure ULg; Delcarte, J.; Jaziri, M. et al

in Journal of Plant Physiology (2002), 159(10),

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See detailOptimization of the expression of heterologous P450 hydroperoxide lyase in Escherichia coli
Delcarte, J.; Jacques, P.; Fauconnier, Marie-Laure ULg et al

Poster (2001, September 11)

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See detailSymposium « Les lipides de Plantes »
Fauconnier, Marie-Laure ULg; Rojas-Beltran, J.; Hoyaux, P. et al

Poster (2001, July 10)

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