Jean-Luc Le Quéré

Dr. Jean-Luc Le Quéré

Centre des Sciences du Goût et de l'Alimentation (CSGA), INRAE, Dijon, France
orcid

Research Focus & Metrics

Academic Career Length

40Years (1987-Present)

(Calculated once Scilit publication data is synced: current year − year of first publication + 1)

Representative Publications

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17 April 1998 in Journal of Agricultural and Food Chemistry
Verified
Journal Article
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IGI. Goubet
I. Goubet
Jean-Luc Le QuéréJean-Luc Le Quéré
Jean-Luc Le Quéré
AVA. J. Voilley
A. J. Voilley

1 February 1996 in Phytochemistry
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Journal Article
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JFJean-Pierre Farine
Jean-Pierre Farine
LLLuc Legal
Luc Legal
BMBrigitte Moreteau
Brigitte Moreteau
Jean-Luc Le QuéréJean-Luc Le Quéré
Jean-Luc Le Quéré

1 July 1991 in Journal of Agricultural and Food Chemistry
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Journal Article
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JBJean Louis Berdague
Jean Louis Berdague
CDChristian Denoyer
Christian Denoyer
Jean-Luc Le QuéréJean-Luc Le Quéré
Jean-Luc Le Quéré
ESEtienne Semon
Etienne Semon

1 April 2000 in Applied and Environmental Microbiology
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Journal Article
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CLCarmen Lapadatescu
Carmen Lapadatescu
CGChristian Giniès
Christian Giniès
Jean-Luc Le QuéréJean-Luc Le Quéré
Jean-Luc Le Quéré
PBPascal Bonnarme
Pascal Bonnarme
Aryl metabolite biosynthesis was studied in the white rot fungus Bjerkandera adusta cultivated in a liquid medium supplemented with l -phenylalanine. Aromatic compounds were analyzed by gas chromatography-mass spectrometry following addition of labelled precursors ( 14 C- and 13 C-labelled l -phenylalanine), which did not interfere with fungal metabolism. The major aromatic compounds identified were benzyl alcohol, benzaldehyde (bitter almond aroma), and benzoic acid. Hydroxy- and methoxybenzylic compounds (alcohols, aldehydes, and acids) were also found in fungal cultures. Intracellular enzymatic activities (phenylalanine ammonia lyase, aryl-alcohol oxidase, aryl-alcohol dehydrogenase, aryl-aldehyde dehydrogenase, lignin peroxidase) and extracellular enzymatic activities (aryl-alcohol oxidase, lignin peroxidase), as well as aromatic compounds, were detected in B. adusta cultures. Metabolite formation required de novo protein biosynthesis. Our results show that l -phenylalanine was deaminated to trans -cinnamic acid by a phenylalanine ammonia lyase and trans -cinnamic acid was in turn converted to aromatic acids (phenylpyruvic, phenylacetic, mandelic, and benzoylformic acids); benzaldehyde was a metabolic intermediate. These acids were transformed into benzaldehyde, benzyl alcohol, and benzoic acid. Our findings support the hypothesis that all of these compounds are intermediates in the biosynthetic pathway from l -phenylalanine to aryl metabolites. Additionally, trans -cinnamic acid can also be transformed via β-oxidation to benzoic acid. This was confirmed by the presence of acetophenone as a β-oxidation degradation intermediate. To our knowledge, this is the first time that a β-oxidation sequence leading to benzoic acid synthesis has been found in a white rot fungus. A novel metabolic scheme for biosynthesis of aryl metabolites from l -phenylalanine is proposed.

1 March 1992 in Journal of Agricultural and Food Chemistry
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Journal Article
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BMBruno. Martin
Bruno. Martin
PEPatrick X. Etievant
Patrick X. Etievant
Jean-Luc Le QuéréJean-Luc Le Quéré
Jean-Luc Le Quéré
PSPascal Schlich
Pascal Schlich

14 January 2004 in Journal of Agricultural and Food Chemistry
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Journal Article
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EPEstelle Pionnier
Estelle Pionnier
CCClaire Chabanet
Claire Chabanet
LMLaurence Mioche
Laurence Mioche
Jean-Luc Le QuéréJean-Luc Le Quéré
Jean-Luc Le Quéré
Christian SallesChristian Salles
Christian Salles