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Registros recuperados: 4
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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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Production of a chimeric enzyme tool associating the Trichoderma reesei swollenin with the Aspergillus niger feruloyl esterase A for release of ferulic acid Inra
LEVASSEUR, A.; Saloheimo, M.; NAVARRO, D.; Andberg, M.; Monot, F.; Nakari-Setälä, T.; ASTHER, M.; RECORD, E..
The main goals of this work were to produce the fusion protein of the Trichoderma reesei swollenin I (SWOI) and Aspergillus niger feruloyl esterase A (FAEA) and to study the effect of the physical association of the fusion partners on the efficiency of the enzyme. The fusion protein was produced up to 25 mg l−1 in the T. reesei strains Rut-C30 and CL847. In parallel, FAEA alone was produced for use as a control protein in application tests. Recombinant FAEA and SWOI–FAEA were purified to homogeneity and characterized. The biochemical and kinetic characteristics of the two recombinant proteins were found to be similar to those of native FAEA, except for the temperature stability and specific activity of the SWOI–FAEA. Finally, the SWOI–FAEA protein was...
Tipo: Journal Article Palavras-chave: ACIDE FERULIQUE; ACIDE COUMARIQUE; SON DE BLE CARBOXYLIC ESTER HYDROLASE; RECOMBINANT FUSION PROTEIN; WHEAT BRAN; FERULOYL ESTERASE; CHIMERIC PROTEIN; SWOLLENIN; BIOTECHNOLOGY; FUNGUS.
Ano: 2006 URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PROD200724ba03ab&uri=/notices/prodinra1/2010/09/
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Tailed giant Tupanvirus possesses the most complete translational apparatus of the known virosphere. Repositório Alice
ABRAHÃO, J.; SILVA, L.; SILVA, L. S.; KHALIL, J. Y. B; RODRIGUES, R.; ARANTES, T.; ASSIS, F.; BORATTO, P.; ANDRADE, M.; KROON, E. G.; RIBEIRO, B.; BERGIER, I.; SELIGMANN, H.; GHIGO, E.; COLSON, P.; LEVASSEUR, A.; KROEMER, G.; RAOULT, D.; LA SCOLA, B..
Here we report the discovery of two Tupanvirus strains, the longest tailed Mimiviridae members isolated in amoebae. Their genomes are 1.44?1.51 Mb linear double-strand DNA coding for 1276?1425 predicted proteins. Tupanviruses share the same ancestors with mimivirus lineages and these giant viruses present the largest translational apparatus within the known virosphere, with up to 70 tRNA, 20 aaRS, 11 factors for all translation steps, and factors related to tRNA/mRNA maturation and ribosome protein modification. Moreover, two sequences with significant similarity to intronic regions of 18 S rRNA genes are encoded by the tupanviruses and highly expressed. In this translation-associated gene set, only the ribosome is lacking. At high multiplicity of...
Tipo: Artigo em periódico indexado (ALICE) Palavras-chave: Virus; Viruses.
Ano: 2018 URL: http://www.alice.cnptia.embrapa.br/alice/handle/doc/1088341
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Tracking the connection between evolutionary and functional shifts using the fungal lipase/feruloyl esterase A family Inra
LEVASSEUR, A.; Gouret, P.; LESAGE-MEESSEN, L.; Asther, M.; ASTHER, M.; RECORD, E.; Pontarotti, P..
BackgroundThere have been many claims of adaptive molecular evolution, but what role does positive selection play in functional divergence? The aim of this study was to test the relationship between evolutionary and functional shifts with special emphasis on the role of the environment. For this purpose, we studied the fungal lipase/feruloyl esterase A family, whose functional diversification makes it a very promising candidate.ResultsThe results suggested functional shift following a duplication event where neofunctionalisation of feruloyl esterase A had occurred with conservation of the ancestral lipase function. Evolutionary shift was detected using the branch-site model for testing positive selection on individual codons along specific lineages....
Tipo: Journal Article Palavras-chave: ADAPTATION MOLECULAIRE; ASPERGILLUS.
Ano: 2006 URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PROD2007ed47815c&uri=/notices/prodinra1/2009/10/
Registros recuperados: 4
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