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Registros recuperados: 6
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Cloning and characterization of a tyrosinase gene from the white-rot fungus Pycnoporus sanguineus, and overproduction of the recombinant protein in Aspergillus niger Inra
Halaouli, S.; Record, E.; Casalot, L.; Hamdi, M.; Sigoillot, J.C.; Lomascolo, A.; Asther, M..
A new tyrosinase-encoding gene (2,204 bp) andthe corresponding cDNA (1,857 nucleotides) from thewhite-rot fungus Pycnoporus sanguineus BRFM49 werecloned. This gene consisted of seven exons and six intronsand encoded a predicted protein of 68 kDa, exceeding themature tyrosinase by 23 kDa. P. sanguineus tyrosinasecDNA was over-expressed in Aspergillus niger, a particularlysuitable fungus for heterologous expression of proteinsof biotechnological interest, under the control ofthe glyceraldehyde-3-phosphate-dehydrogenase promoteras strong and constitutive promoter. The glucoamylasepreprosequence of A. niger was used to target the secretion.This construction enabled the production of recombinanttyrosinase in the extracellular medium of A. niger. Theidentity of...
Tipo: Journal Article Palavras-chave: FUNGAL TYROSINASE.
Ano: 2006 URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PROD20078d7fe834&uri=/notices/prodinra1/2010/09/
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Enzymatic saccharification of wheat straw for bioethanol production by a combined cellulase xylanase and feruloyl esterase treatment Inra
Tabka, M.G.; Herpoël-Gimbert, I.; Monod, F.; Asther, M.; Sigoillot, J.C..
The focus of this study was to improve conditions of use of fungal lignocellulolytic enzymes for conversion of lignocellulosic biomass to fermentable sugars for the production of bioethanol.Wheat straw was pre-treated by acid treatment with diluted sulfuric acid followed by steam explosion. Several enzymatic treatments implementing hydrolases (cellulases and xylanases from Trichoderma reesei, recombinant feruloyl esterase (FAE) from Aspergillus niger and oxidoreductases (laccases from Pycnoporus cinnabarinus) were investigated to the saccharification of exploded wheat straw. A synergistic effect between cellulases, FAE and xylanase was proven under a critical enzymatic concentration (10 U/g of cellulases, 3 U/g of xylanase and 10 U/g of FAE). The yield of...
Tipo: Journal Article Palavras-chave: ENZYME LIGNOLITIQUE FUNGAL ENZYME; SACCHARIFICATION; WHEAT STRAW; BIOETHANOL.
Ano: 2006 URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PROD2008ea41c692&uri=/notices/prodinra1/2008/06/
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Natural and recombinant fungal laccases for paper pulp bleaching Inra
Sigoillot, C.; RECORD, E.; Belle, V.; ROBERT, J.L.; LEVASSEUR, A.; Punt, P.J.; Van Den Hondel, C.A.M.J.J.; Fournel, A.; Sigoillot, J.C.; ASTHER, M..
Three laccases, a natural form and two recombinant forms obtained from two different expression hosts, were characterized and compared for paper pulp bleaching. Laccase from Pycnoporus cinnabarinus, a well known lignolytic fungus, was selected as a reference for this study. The corresponding recombinant laccases were produced in Aspergillus oryzae and A. niger hosts using the lacI gene from P. cinnabarinus to develop a production process without using the expensive laccase inducers required by the native source. In flasks, production of recombinant enzymes by Aspergilli strains gave yields close to 80 mg l–1. Each protein was purified to homogeneity and characterized, demonstrating that the three hosts produced proteins with similar physico-chemical...
Tipo: Journal Article Palavras-chave: PULPE DE PAPIER; BIOTECHNOLOGIE INDUSTRIELLE; PROPRIETE PHYSICOCHIMIQUE LACCASE; RECOMBINANT PROTEIN.
Ano: 2004 URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PROD2007a0177074&uri=/notices/prodinra1/2010/09/
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Overproduction of the Aspergillus niger feruloyl esterase for pulp bleaching application Inra
Record, E.; Asther, M.; Sigoillot, J.C.; Pagès, S.; Punt, P.J.; Delattre, M.; Haon, M.; Van den Hondel, C.A.M.J.J.; Sigoillot, J.C.; Lesage-Meessen, L.; Asther, M..
A well-known industrial fungus for enzyme production, Aspergillus niger, was selected to produce the feruloyl esterase FAEA by homologous overexpression for pulp bleaching application. The gpd gene promoter was used to drive FAEA expression. Changing the nature and concentration of the carbon source nature (maltose to glucose; from 2.5 to 60 g l(-1)), improved FAEA activity 24.5-fold and a yield of 1 g l(-1) of the corresponding protein in the culture medium was achieved. The secreted FAEA was purified 3.5-fold to homogeneity in a two-step purification procedure with a recovery of 69%. The overproduced protein was characterised and presented properties in good agreement with those of native FAEA. The recombinant FAEA was tested for wheat straw pulp...
Tipo: Journal Article Palavras-chave: BLANCHIMENT FERULOYL ESTERASE; WHEAT-STRAW PULP; ENZYMATIC TREATMENT; LACCASE; XYLANASE.
Ano: 2003 URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PROD20071bf46680&uri=/notices/prodinra1/2010/09/
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Role of ethanol on growth, laccase production and protease activity in Pycnoporus cinnabarinus ss3 Inra
Meza, J.C.; Auria, R.; Lomascolo, A.; Sigoillot, J.C.; Casalot, L..
Laccase production by the strain Pycnoporus cinnabarinus ss3 was studied in a solid-state culture on sugar-cane bagasse using chemical compounds as inducers (ethanol, methanol, veratryl alcohol and ferulic acid). Laccase productions were about 5- to 8.5-fold higher than non-induced cultures.Liquid-culture experiments with 14C-labeled ethanol were conducted. Ninety-eight percent of the initial amount of 14C from ethanol was recovered as 14CO2, 14C-biomass and soluble 14C-compounds (mainly ethanol). The amount of 14C in the biomass was only 6.8% of the total carbon consumed by P. cinnabarinus, in absence of maltose, representing only 2.8% of added ethanol (1.1% and 1.6% in presence of maltose, respectively). Ethanol was poorly used as carbon and energy...
Tipo: Journal Article Palavras-chave: ENZYME PROTEOLYTIQUE; ACTIVITE ENZYMATIQUE PYCNOPORUS CINNABARINUS.
Ano: 2007 URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PROD20086cc0fa6a&uri=/notices/prodinra1/2008/06/
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Secretome analysis of Phanerochaete chrysosporium strains CIRM-BRFM41 grown on softwood Inra
Ravalason, H.; Jan, G.; Mollé, D.; Pasco, M.; Coutinho, P.M.; Lapierre, C.; Pollet, B.; Bertaud, F.; Petit-Conil, M.; Grisel, S.; Sigoillot, J.C.; Asther, M.; Gimbert, I..
Abstract Proteomic analysis was performed to determine and differentiate the composition of the secretomes of Phanerochaete chrysosporium CIRM-BRFM41, a peroxidasehypersecretory strain grown under ligninolytic conditions and on softwood chips under biopulping conditions.Extracellular proteins from both cultures were analyzed by bidimensional gel electrophoresis and matrix-assisted laserdesorption/ionization time-of-flight tandem mass spectrometry.A total of 37 spots were identified. The secretome in liquid synthetic medium comprised mainly peroxidases,while several wood-degrading enzymes and enzymes involved in fungal metabolism were detected in biopulping cultures on softwood. This prompted an analysis of the impact of secretome modulation in the presence...
Tipo: Journal Article Palavras-chave:  SECRETOME SOFTWOOD CHEMICAL PULPING; Phanerochaete chrysosporium.
Ano: 2008 URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PROD20092bd81e9f&uri=/notices/prodinra1/2010/09/
Registros recuperados: 6
Primeira ... 1 ... Última
 

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