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Effects of propiconazole on extra-cellular enzymes involved in nutrient mobilization during Trametes versicolor wood colonization Inra
Lekounougou, S.; Jacquot, J.P.; Gérardin, P.; Gelhaye, É..
The effects of propiconazole on extra-cellular enzyme levels in Trametes versicolor have been investigated during wood colonization and degradation. The working hypothesis was that the biocide could alter metabolic pathways, which could lead to an alteration of extra-cellular enzyme production. In the presence of a propiconazole sub-lethal concentration, the wood degradation rate decrease concomitantly with the lag phase of fungal development observed during wood colonisation. The pattern of production of enzymes involved in polysaccharide degradation (b-glucosidases, glucuronidases, cellobiohydrolases), nitrogen (leucine aminopeptidase) and phosphorus (acid phosphatase) mobilization was only slightly altered in the presence of the biocide. In experiments...
Tipo: Journal Article Palavras-chave: PROPICONAZOLE; TRIAZOLE; CHAMPIGNON LIGNIVORE; TRAITEMENT CHIMIQUE; MECANISME ACTION; ENZYME EXTRA-CELLULAIRE; B-GLUCOSIDASE; GLUCURONIDASE; B-CELLOBIOSIDASE; LEUCINE AMINOPEPTIDASE; PHOSPHATASE ACIDE; CHITINASE; CAFEINE; CROISSANCE FONGIQUE; INHIBITION; PRESERVATION DU BOIS ACID PHOSPHATASE; BETA-GLUCOSIDASE; BIOCIDES; CAFFEINE; CHITINASE; COLONIZATION; ENZYME ACTIVITY; ENZYMES; MICROBIAL DEGRADATION; MOBILIZATION; NUTRIENTS; PROPICONAZOLE; WOOD PRESERVATION.
Ano: 2008 URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PROD2010d5b49ffa&uri=/notices/prodinra1/2010/11/
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Proteolytic activity in Encephalitozoon cuniculi sporogonial stages : Predominance of metallopeptidases including an aminopeptidase-P-like enzyme Inra
Chavant, P.; Taupin, V.; El Alaoui, H.; Wawrzyniak, I.; Chambon, C.; Prensier, G.; Méténier, G.; Vivarès, C.P..
A fraction enriched in spore precursor cells (sporoblasts) of the microsporidian Encephalitozoon cuniculi, an intracellular parasite of mammals, was obtained by Percoll gradient centrifugation. Soluble extracts of these cells exhibited proteolytic activity towards azocasein, with an alkaline optimum pH range (9-10). Prevalence of some metallopeptidases was supported by the stimulating effect of Ca2+, Mg2+, Mn2+ and Zn2+ ions. and inhibition by two chelating agents (EDTA and 1,10-phenanthroline), a thiol reductant (dithiothreitol) and two aminopeptidase inhibitors (bestatin and apstatin). Zymographic analysis revealed four caseinolytic bands at about 76, 70, 55 and 50 kDa. Mass spectrometry of tryptic peptides from one-dimensional gel slices identified a...
Tipo: Journal Article Palavras-chave: MICROSPORA; LEUCINE MICROSPORIDIA; ENCEPHALITOZOON CUNICULI; PROTEOLYTIC ACTIVITY; AMINOPEPTIDASE P; LEUCINE AMINOPEPTIDASE.
Ano: 2005 URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PROD2007461284f7&uri=/notices/prodinra1/2007/07/
Registros recuperados: 2
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