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dc.creatorFesta, Giovannaes_ES
dc.creatorGiardina, Paolaes_ES
dc.creatorFaraco, Vicenzaes_ES
dc.creatorPiscitelli, Alessandraes_ES
dc.creatorSannia, Giovannies_ES
dc.date.accessioned2018-02-14T09:31:32Z
dc.date.available2018-02-14T09:31:32Z
dc.date.issued2006
dc.identifier.isbn84-9769-107-5
dc.identifier.urihttps://hdl.handle.net/2454/27225
dc.descriptionComunicación presentada 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.es_ES
dc.description.abstractWhite-rot fungi are the most efficient decomposers of lignocellulose because of their capability to synthesize the relevant hydrolytic (cellulases and hemicellulases) and oxidative (laccases, lignin-peroxidases and Mn-peroxidases) extracellular enzymes required to degrade the major components of substrates (cellulose, hemicellulose, and lignin) into low-molecular-weight compounds that can be assimilated in fungal nutrition [1]. Recently, extensive research on these fungi has been conducted with the aim of isolating new organisms able to secrete new enzymes with capability to be used in industrial applications, such as bioremediation of polluted soils and industrial waste-waters, biobleaching and biopulping in pulp and paper industries, textile and food industries, etc. Fungal laccases (benzenediol: oxygen oxidoreductases; EC1.10.3.2) are ligninolytic enzymes that have been isolated from various fungi [2]. They belong to the class of the blue oxidases containing 4 copper atoms/molecule distributed in three different copper binding sites [3, 4]. The type-1 site is responsible for the intense blue colour of the enzyme due to a maximum absorbance at 605 nm; the type-2 site does not exhibit signals in the visible absorbance spectrum; and the type-3 site incorporates two copper centres and is responsible for a band near 330 nm. All these copper ions are involved in the catalytic mechanism. Laccases reduce oxygen to water and simultaneously perform a one electron oxidation of aromatic substrates (polyphenols, methoxysubstituted monophenols, aromatic amines, etc.). These enzymes are present in multiple isoforms, depending on the fungal species and environmental growth conditions [5, 6].en
dc.description.sponsorshipThis work was supported by grants from the Ministero dell’Università e della Ricerca Scientifica (Progetti di Rilevante Interesse Nazionale, PRIN) and from EC FP6 Project SOPHIED (NMP2-CT-2004-505899).en
dc.format.extent15 p.
dc.format.mimetypeapplication/pdfen
dc.language.isoengen
dc.publisherUniversidad Pública de Navarra / Nafarroako Unibertsitate Publikoaes
dc.relation.ispartofAntonio 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.es
dc.rights© Autores; Universidad Pública de Navarra. Esta publicación no puede ser reproducida, almacenada o transmitida total o parcialmente, sea cual fuere el medio y el procedimiento, incluidas las fotocopias, sin permiso previo concedido por escrito por los titulares del copyright.es_ES
dc.subjectLaccasesen
dc.subjectPleorotus ostreatusen
dc.subjectIndustrial applicationsen
dc.titleAtypical laccases from the white-rot fungus Pleurotus ostreatus and their application for the treatment of industrial coloured effluentsen
dc.typeinfo:eu-repo/semantics/conferenceObjecten
dc.typeContribución a congreso / Biltzarrerako ekarpenaes
dc.rights.accessRightsinfo:eu-repo/semantics/openAccessen
dc.rights.accessRightsAcceso abierto / Sarbide irekiaes
dc.type.versioninfo:eu-repo/semantics/publishedVersionen
dc.type.versionVersión publicada / Argitaratu den bertsioaes


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