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Construction of engineered bifunctional enzymes and their overproduction in Aspergillus niger for improved enzymatic tools to degrade agricultural by-products Inra
Levasseur, A.; Navarro, D.; Punt, P.J.; Belaïch, J.P.; Asther, M.; Record, E..
Two chimeric enzymes, FLX and FLXLC, were designed and successfully overproduced in Aspergillus niger. FLX construct is composed of the sequences encoding the feruloyl esterase A (FAEA) fused to the endoxylanase B (XYNB) of A. niger. A C-terminal carbohydrate-binding module (CBM family 1) was grafted to FLX, generating the second hybrid enzyme, FLXLC. Between each partner, a hyperglycosylated linker was included to stabilize the constructs. Hybrid proteins were purified to homogeneity, and molecular masses were estimated to be 72 and 97 kDa for FLX and FLXLC, respectively. Integrity of hybrid enzymes was checked by immunodetection that showed a single form by using antibodies raised against FAEA and polyhistidine tag. Physicochemical properties of each...
Tipo: Journal Article Palavras-chave: SON DE CEREALE; ACTIVITE ENZYMATIQUE ASPERGILLUS NIGER.
Ano: 2005 URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PROD20086808f0a6&uri=/notices/prodinra1/2008/08/
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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/
Registros recuperados: 3
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