Zobrazeno 1 - 10
of 14
pro vyhledávání: '"Philippe Colin-Morel"'
Publikováno v:
Food chemistry. 227
Many researchers have focused on high molecular weight (Mw) exopolysaccharides (EPS) as a source of potentially bioactive lower Mw derivatives. Therefore, it is of interest to find means for efficient and safe production of depolymerized-polymer deri
Autor:
A. Da Costa, Philippe Colin-Morel, Bernard Courtois, Josiane Courtois, Philippe Michaud, Alain Heyraud
Publikováno v:
Carbohydrate Polymers. 51:223-228
The Sinorhizobium meliloti M5N1CS strain produces during fermentation a polyglucuronan and oligoglucuronans β-(1→4) linked and partially acetylated. Following the detection of unsaturated oligoglucuronans in the culture media, a glucuronan lyase (
Autor:
Jean-Marc Simonet, Claude Bosso, Cécile Vanhaverbeke, Lynda Gamar-Nourani, Claude Gey, Karine Blondeau, Alain Heyraud, Philippe Colin-Morel
Publikováno v:
Carbohydrate Research. 314:211-220
The extracellular polysaccharide produced by Lactobacillus rhamnosus strain C83 was found to be composed of D-glucose and D-galactose in a molar ratio of 2:3. The primary structure of the polysaccharide was shown by sugar analysis, methylation analys
Autor:
Josiane Courtois, M. L. Gonzales, Jean-Noël Barbotin, Philippe Colin-Morel, Bernard Courtois, Alain Heyraud, Philippe Michaud
Publikováno v:
Annals of the New York Academy of Sciences. 782:53-60
Autor:
Alain Heyraud, J. P. Seguin, Josiane Courtois, Philippe Colin-Morel, Bernard Courtois, Jean-Noël Barbotin, Philippe Michaud
Publikováno v:
International Journal of Biological Macromolecules. 17:369-372
During fermentation, the mutant strain Rhizobium mefliloti M5N1 CS, which induces nodule formation on alfalfa roots, produces a partially acetylated (1 → 4)-β-d-glucuronan. In addition to this exopolysaccharide of high molecular weight, the mutant
Autor:
Alain Heyraud, Jean-Noël Barbotin, J. P. Seguin, Josiane Courtois, Philippe Michaud, Philippe Colin-Morel, Bernard Courtois
Publikováno v:
International Journal of Biological Macromolecules. 16:301-305
The mutant Rhizobium meliloti M5N1CS (NCIMB 40472) produced a partially acetylated (1→4)-β-d-glucuronan during fermentation. The polysaccharide (EPS) extracted from broth during fermentation by microfiltration and ultrafiltration (using a 100 kDa
Autor:
Sophie Declomesnil, Luciana Dantas, Alain Heyraud, Jean-Noël Barbotin, J. P. Seguin, Bernard Courtois, Josiane Courtois, Philippe Colin-Morel
Publikováno v:
Journal of Carbohydrate Chemistry. 12:441-448
A mutant of the R. meliloti M5N1 strain has been selected. This strain, R. meliloti M5N1 CS (NCIMB 40472), excretes an extracellular material composed of 2-O-Ac-β-GlcpA, 3-O-Ac-β-GlcpA, 2,3-di-O-Ac-β-GlcpA and three species of β-GlcpA residues 1
Autor:
Micheline Guinand, Alain Heyraud, Frederic Chavagnat, Jean Wallach, Philippe Colin-Morel, Claude Gey
Publikováno v:
ChemInform. 29
Two Pseudomonas aeruginosa alginates were lysed by an overexpressed polymannuronate lyase AlxM B (only acting on two or more consecutive, nonacetylated mannuronate units) to prepare either mannuronate blocks (poly-M blocks) with dp∼30, or strictly
Autor:
Philippe Colin-Morel, Bernard Courtois, Philippe Michaud, Alexandre Da Costa, Josiane Courtois, Alain Heyraud, Emmanuel Petit
Publikováno v:
Applied and Environmental Microbiology
Applied and Environmental Microbiology, American Society for Microbiology, 2001, pp.5197-5203
Scopus-Elsevier
Applied and Environmental Microbiology, American Society for Microbiology, 2001, pp.5197-5203
Scopus-Elsevier
A glucuronan lyase extracted from Sinorhizobium meliloti strain M5N1CS was purified to homogeneity by anion-exchange chromatography. The purified enzyme corresponds to a monomer with a molecular mass of 20 kDa and a pI of 4.9. A specific activity was
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f7a26abee5d91b06a5e8998583eba0c7
https://hal.archives-ouvertes.fr/hal-00307665
https://hal.archives-ouvertes.fr/hal-00307665
Publikováno v:
Carbohydrate research. 308(3-4)
Lysis of alginates and of their saturated and unsaturated fragments was monitored by 1H NMR spectroscopy. AlxM(B) alginate lyase performs beta-elimination on the mannuronic acid (M) residues. It does not cleave the guluronic acid (G) sequences, nor t