Cellobiohydrolase
Mostrando 1-12 de 58 artigos, teses e dissertações.
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1. Caracterização bioquímica, biofísica e estrutural da Celobiohidrolase I de Trichoderma harzianum / Biochemical, biophysical and structural characterization of Cellobiohydrolase I from Trichoderma harzianum
Devido à sua importante atividade celulolítica, o fungo Trichoderma harzianum possui um grande potencial de aplicação na hidrólise da biomassa. No entanto, as celulases deste fungo filamentoso ainda não foram caracterizadas em profundidade. A celobiohidrolase I (CBHI) é a principal enzima celulolítica produzida por Trichoderma sp. e atualmente é uma
IBICT - Instituto Brasileiro de Informação em Ciência e Tecnologia. Publicado em: 01/10/2012
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2. Caracterização bioquímica e biofísica da Celobiohidrolase II do fungo Trichoderma harzianum IOC3844 produzida por expressão homóloga / Biochemical and biophysical characterization of cellobiohydrolase II from Trichoderma harzianum IOC 3844 produced by homologous expression
The depletion of reserves, especially of refined oil , with increased energy demands and the urgent need to reduce the carbon emissions on the atmosphere, signals the necessity to search for new sources of energy renewable and clean. Concerns about global warming have led to an increased world interest in biofuels. The new concept of second generation biofue
IBICT - Instituto Brasileiro de Informação em Ciência e Tecnologia. Publicado em: 30/07/2012
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3. Integrated experimental biophysics and molecular dynamics simulations of biomolecules in solution - the interaction of nuclear receptors with DNA response elements and the inter-domain dynamics of Cellobiohydrolase I / Estudos por modelagem e dinâmica molecular integradas a técnicas físicas para biomoléculas em solução - interação de receptores nucleares a elementos responsivos no DNA e dinâmica inter-domínios da celobiohidrolase I
Collective motions play a fundamental role in solution biomolecule dynamics and energetics. These movements can couple very distant regions in the protein structures affection, for instance, allosteric mechanisms, the establishment of macromolecular complexes, and on the integrated function of multidomain proteins as molecullar machines. In this thesis, we p
IBICT - Instituto Brasileiro de Informação em Ciência e Tecnologia. Publicado em: 26/09/2011
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4. Identificação de transcritos de Ceriporiopsis subvermispora expressos nas fases iniciais da biodegradação da madeira / Identification of transcripts of Ceriporiosis subvermispora expressed during initial phases of wood biodegradation
Lignin is a heterogeneous and highly cross-linked macromolecule that is particularly resistant to biological degradation but some specialized fungi developed the ability to degrade this complex molecule. Most of these fungi belong to the basidiomycetes and are responsible for the white-rot decay processo One of them, Ceriporiopsis subvermispora, has been ext
Publicado em: 2006
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5. Mechanism by which cellulose triggers cellobiohydrolase I gene expression in Trichoderma reesei.
The expression of cellobiohydrolase I mRNA from Trichoderma reesei, measured by Northern blot hybridization, is controlled by the nature of carbon sources used in the culture medium. Cellulose and the soluble disaccharide sophorose, but not glycerol or glucose, act as inducers. Cellobiohydrolase I mRNA was undetectable when antibodies to the major members of
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6. Isolation and properties of a major cellobiohydrolase from the cellulosome of Clostridium thermocellum.
In the anaerobic, thermophilic, cellulolytic bacterium Clostridium thermocellum, efficient solubilization of the insoluble cellulose substrate is accomplished largely through the action of a cellulose-binding multienzyme complex, the cellulosome. A major cellobiohydrolase activity from the cellulosome has been traced to its Mr 75,000 S8 subunit, and an activ
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7. Phanerochaete chrysosporium Cellobiohydrolase and Cellobiose Dehydrogenase Transcripts in Wood
The transcripts of structurally related cellobiohydrolase genes in Phanerochaete chrysosporium-colonized wood chips were quantified. The transcript patterns obtained were dramatically different from the transcript patterns obtained previously in defined media. Cellobiose dehydrogenase transcripts were also detected, which is consistent with the hypothesis th
American Society for Microbiology.
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8. Double-Antibody Sandwich Enzyme-Linked Immunosorbent Assay for Cellobiohydrolase I
A double-antibody sandwich enzyme-linked immunosorbent assay was developed for quantifying cellobiohydrolase I (CBH I) in crude preparations of the cellulase complex from Trichoderma reesei. The other enzymes (endoglucanase and β-glucosidase) in this complex and other ingredients in culture broth did not interfere with this assay. The antibody configuration
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9. Structure, organization, and transcription of a cellobiohydrolase gene cluster from Phanerochaete chrysosporium.
Restriction mapping and sequence analysis of cosmid clones revealed a cluster of three cellobiohydrolase genes in Phanerochaete chrysosporium. P. chrysosporium cbh1-1 and cbh1-2 are separated by only 750 bp and are located approximately 14 kb upstream from a cellulase gene previously cloned from P. chrysosporium (P. Sims, C. James, and P. Broda, Gene 74:411-
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10. Nucleotide sequence of the cellobiohydrolase gene from Trichoderma viride.
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11. The cellulose-binding domain of the major cellobiohydrolase of Trichoderma reesei exhibits true reversibility and a high exchange rate on crystalline cellulose.
Cellulose-binding domains (CBDs) bind specifically to cellulose, and form distinct domains of most cellulose degrading enzymes. The CBD-mediated binding of the enzyme has a fundamental role in the hydrolysis of the solid cellulose substrate. In this work we have investigated the reversibility and kinetics of the binding of the CBD from Trichoderma reesei cel
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12. Production of Trichoderma reesei cellulases on glucose-containing media.
The filamentous fungus Trichoderma reesei was shown to secrete active cellobiohydrolase I and the endoglucanase I catalytic core domain into the culture medium when the fungus was grown on glucose-containing medium. The expression of the proteins was driven by the promoters of the elongation factor 1 alpha, tef1, and the unidentified gene for cDNA1. The cDNA