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    Molecular characterization of A cellobiohydrolase gene family in the fungus Pleurotus ostreatus

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    PA03_Molecular.pdf (64.40Kb)
    Fecha
    2006
    Autor
    Eizmendi Goicoechea, Arantza 
    Sannia, G. 
    Ramírez Nasto, Lucía Upna
    Pisabarro de Lucas, Gerardo Upna
    Versión
    Acceso abierto / Sarbide irekia
    xmlui.dri2xhtml.METS-1.0.item-type
    Contribución a congreso / Biltzarrerako ekarpena
    Versión
    Versión publicada / Argitaratu den bertsioa
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    Resumen
    Cellulose is the most abundant biological polymer on Earth. Its chemical composition consists of D-glucose units linked by β-1,4- glycosidic bonds forming linear polymeric chains with a reducing and a non-reducing end. Cellulose chains may either adhere to each other, via hydrophobic and van der Waals interactions, forming crystalline structures or remain more loosely packaged (amorphous cellulos ... [++]
    Cellulose is the most abundant biological polymer on Earth. Its chemical composition consists of D-glucose units linked by β-1,4- glycosidic bonds forming linear polymeric chains with a reducing and a non-reducing end. Cellulose chains may either adhere to each other, via hydrophobic and van der Waals interactions, forming crystalline structures or remain more loosely packaged (amorphous cellulose). Consequently, the physical structure and morphology of native cellulose is complex and not uniform. Biological degradation of cellulose depends on the action of three types of enzymes: endoglucanases (E.C.3.2.1.4), cellobiohydrolases (E.C.3.2.1.91) and β-glucosidases (E.C.3.2.1.21). All them hydrolyse β-1,4-glycosidic bonds but they differ on the substrate specificity. Endoglucanases hydrolyse the amorphous regions of the cellulose fibbers generating new reducing and non-reducing ends, cellobiohydrolases attack the molecule ends yielding cellobiose units, and β-glucosidases hydrolyse cellobiose molecules yielding glucose. Cellobiohydrolases can be classified into two groups: type I (CBHI) and type II (CBHII), each having opposite chain-end specificities. CBHI prefer the reducing ends while CBHII act at non-reducing ends. By the screening of a genomic library from the basidiomycete Pleurotus ostreatus var. florida, we have isolated five cbhI genes, named cbhI1, cbhI2, cbhI3, cbhI4 and cbhI5, proving the occurrence of a multigenic family coding for this enzymatic activity. Using this sequences as probe, it has been possible to know the conditions in which are expressed those genes. This has allowed the synthesis of the each gene cDNA and, by comparison of this sequence with the corresponding genomic sequence, the characterization of their structure. On the other hand, using the RFLP technique and a progeny of 80 monokaryons derived from the dikaryon N001, the five genes have been mapped on the linkage map of P. ostreatus var. florida mapping the cbhI1 to the chromosome IV and the others to the chromosome VI. [--]
    Materias
    Pleurotus ostreatus, Cellobiohydrolases
     
    Editor
    Universidad Pública de Navarra / Nafarroako Unibertsitate Publikoa
    Publicado en
    Antonio G. Pisabarro and Lucía Ramírez (eds.): VI Meeting on Genetics and Cellular Biology of Basidiomycetes (GCBB-VI). Pamplona: Universidad Pública de Navarra / Nafarroako Unibertsitate Publikoa, 2006.
    Notas
    Resumen del poster presentado al VI Meeting on Genetics and Cellular Biology of Basidiomycetes (GCBB-VI), organizado por y celebrado en la Universidad Pública de Navarra el 3-6 de junio de 2005.
    Departamento
    Universidad Pública de Navarra. Departamento de Producción Agraria / Nafarroako Unibertsitate Publikoa. Nekazaritza Ekoizpena Saila
     
    URI
    https://hdl.handle.net/2454/27260
    Entidades Financiadoras
     
    Aparece en las colecciones
    • VI Meeting on Genetics and Cellular Biology of Basidiomycetes (GCBB-VI) [60]
    • Comunicaciones y ponencias de congresos - Biltzarrak eta Argitalpenak [328]
    • Comunicaciones y ponencias de congresos DPA - NES Biltzarretako komunikazioak eta txostenak [12]
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     © Universidad Pública de Navarra - Nafarroako Unibertsitate Publikoa
         Repositorio basado en DSpace

    Contacto | Sugerencias