Zobrazeno 1 - 10
of 43
pro vyhledávání: '"Christian Gaudin"'
Autor:
Wadih Ghattas, Michel Giorgi, Christian Gaudin, Antal Rockenbauer, Marius Réglier, A. Jalila Simaan
Publikováno v:
Bioinorganic Chemistry and Applications, Vol 2007 (2007)
Two copper(II)-ACC complexes were prepared and characterized: [Cu(bpy)(ACC)(H2O)]⋅CO4 (1) and [Cu(ACC)2]3⋅4H2O (2). Their crystallographic structures are described and analyzed. Spectroscopic characterizations (UV-visible and EPR) confirm that th
Externí odkaz:
https://doaj.org/article/138592a1cc3d4281aee511c93b341b51
Autor:
Vincent Gaydou, Thierry Tron, Christian Gaudin, Gisela Ertel, Gilles Iacazio, Sylvain Tranchimand
Publikováno v:
Biochimie. 90:781-789
Quercetinase (quercetin 2,3-dioxygenase, EC 1.13.11.24) is produced by various filamentous fungi when grown on rutin as the sole carbon and energy source. From a rutin based liquid culture of Penicillium olsonii, we purified a quercetinase with a spe
Publikováno v:
Journal of Molecular Catalysis B: Enzymatic. 42:27-31
We report here on the use of a biphasic reaction solvent during the laccase catalysed transformation of sinapinic and ferulic acids. As compared to buffer alone, higher product selectivity, higher yields and higher product stability were obtained sim
Publikováno v:
FEMS Microbiology Letters. 253:289-294
Quercetinase is produced by various filamentous fungi when grown on rutin as sole carbon and energy source. We investigated on the effect of 10 phenolics and two sugars, structurally related to substrates and products of the rutin catabolic pathway,
Autor:
Christian Gaudin, Marius Réglier, Agnieszka Klonowska, André Fournel, Thierry Tron, Marcel Asso
Publikováno v:
Enzyme and Microbial Technology. 36:34-41
Trametes sp. strain C30 modulates the synthesis of various laccase isoforms in response to external stimuli. Systematic cloning and heterologous expression of laccase cDNAs were carried out to find C30 enzymes with high oxidative capacities. Two cDNA
Autor:
Thierry Tron, Agnieszka Klonowska, André Fournel, Christian Gaudin, Marcel Asso, Jean Petit, Michel Giorgi
Publikováno v:
European Journal of Biochemistry. 269:6119-6125
A new exocellular laccase was purified from the basidiomycete C30. LAC2 is an acidic protein (pI = 3.2) preferentially produced upon a combined induction by copper and p-hydroxybenzoate. The spectroscopic signature (UV/visible and EPR) of this isofor
Autor:
Chantal Tardif, Christian Gaudin, Sandrine Pagès, Anne Belaich, Laurent Gal, Jean-Pierre Belaich
Publikováno v:
Journal of Bacteriology
Journal of Bacteriology, American Society for Microbiology, 1997, 179 (21), pp.6595-6601. ⟨10.1128/jb.179.21.6595-6601.1997⟩
Journal of Bacteriology, 1997, 179 (21), pp.6595-6601. ⟨10.1128/jb.179.21.6595-6601.1997⟩
Journal of Bacteriology, American Society for Microbiology, 1997, 179 (21), pp.6595-6601. ⟨10.1128/jb.179.21.6595-6601.1997⟩
Journal of Bacteriology, 1997, 179 (21), pp.6595-6601. ⟨10.1128/jb.179.21.6595-6601.1997⟩
International audience; The gene coding for CelG, a family 9 cellulase from Clostridium cellulolyticum, was cloned and overexpressed in Escherichia coli. Four different forms of the protein were genetically engineered, purified, and studied: CelGL (t
Publikováno v:
Journal of Biotechnology. 57:3-14
Recent findings on the cellulolytic system of the mesophilic Clostridium cellulolyticum are reviewed. Six cellulases and the scaffolding protein, which are, at the present time, the known components of the cellulosome have been cloned. The catalytic
Autor:
C Reverbel-Leroy, Christian Gaudin, Alain Bernadac, Anne Belaich, Chantal Tardif, Jean-Pierre Belaich
Publikováno v:
Microbiology. 142:1013-1023
The CelF-encoding sequence was isolated from Clostridium cellulolyticum genomic DNA using the inverse PCR technique. The gene lies between cipC (the gene encoding the cellulosome scaffolding protein) and celC (coding for the endoglucanase C) in the l
Autor:
Anne Belaich, Jean Pierre Belaich, Christian Gaudin, Mirjam Czjzek, Richard Haser, Valérie M.-A. Ducros, Henri Pierre Fierobe, Gideon J. Davies
Publikováno v:
Structure. 3:939-949
Background: Cellulases are glycosyl hydrolases — enzymes that hydrolyze glycosidic bonds. They have been widely studied using biochemical and microbiological techniques and have attracted industrial interest because of their potential in biomass co