Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Christian Gaudin"'
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
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:
Christian Gaudin, Sandrine Pagès, Laurent Gal, Anne Belaich, Chantal Tardif, Jean-Pierre Belaich
Publikováno v:
Journal of Bacteriology
Journal of Bacteriology, 1997, 179 (9), pp.2810-2816. ⟨10.1128/jb.179.9.2810-2816.1997⟩
Journal of Bacteriology, American Society for Microbiology, 1997, 179 (9), pp.2810-2816. ⟨10.1128/jb.179.9.2810-2816.1997⟩
Journal of Bacteriology, 1997, 179 (9), pp.2810-2816. ⟨10.1128/jb.179.9.2810-2816.1997⟩
Journal of Bacteriology, American Society for Microbiology, 1997, 179 (9), pp.2810-2816. ⟨10.1128/jb.179.9.2810-2816.1997⟩
International audience; The role of a miniscaffolding protein, miniCipC1, forming part of Clostridium cellulolyticum scaffolding protein CipC in insoluble cellulose degradation was investigated. The parameters of the binding of miniCipC1, which conta
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0c4888e6dc49242ed288e3bc26e729d6
https://institut-agro-dijon.hal.science/hal-02007516
https://institut-agro-dijon.hal.science/hal-02007516
Publikováno v:
Applied and environmental microbiology. 61(9)
A 43-kDa beta-xylosidase from Clostridium cellulolyticum was purified to homogeneity. The enzyme releases xylose from p-nitrophenylxylose and xylodextrins with a degree of polymerization ranging between 2 and 5. The N-terminal amino acid sequence of
The 1.6 A resolution crystal structure of the catalytic domain of family 5 of glycosyl hydrolases, the endoglucanase CelCCA from Clostridium cellulolyticum , is reported. The structural fold belongs to the superfamily of (α/β)8-barrel enzymes, with
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::aa071e73d8792904868eb620be66e9b7
https://doi.org/10.1016/s0921-0423(06)80107-3
https://doi.org/10.1016/s0921-0423(06)80107-3
Autor:
Chantal Bagnara-Tardif, Christian Gaudin, Françoise Guerlesquin, Henri-Pierre Fierobe, Paul Sauve, Jean-Pierre Belaich, Anne Belaich
Publikováno v:
European journal of biochemistry. 217(2)
An Escherichia coli clone was constructed to overproduce endoglucanase C (CelCCC) from Clostridium cellulolyticum. This construction made it easier to isolate the enzyme but, as observed in the case of endoglucanase A (CelCCA) from the same organism,