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dc.contributor.authorCopete, Ledys S.es_ES
dc.contributor.authorChanagá, Xiomaraes_ES
dc.contributor.authorBarriuso, Jorgees_ES
dc.contributor.authorLópez-Lucendo, María F.es_ES
dc.contributor.authorMartínez, María Jesúses_ES
dc.contributor.authorCamarero, Susanaes_ES
dc.date.issued2015-07-29-
dc.identifier.citationBMC Biotechnology 15: 74 (2015)es_ES
dc.identifier.issn1472-6750-
dc.identifier.urihttp://hdl.handle.net/10261/121528-
dc.description13 p.-4 fig.-4 tab.es_ES
dc.description.abstract[Background] Fungal laccases are multicopper oxidases (MCOs) with high biotechnological potential due to their capability to oxidize a wide range of aromatic contaminants using oxygen from the air. Albeit the numerous laccase-like genes described in ascomycete fungi, ascomycete laccases have been less thoroughly studied than white-rot basidiomycetous laccases. A variety of MCO genes has recently been discovered in plant pathogenic ascomycete fungi, however little is known about the presence and function of laccases in these fungi or their potential use as biocatalysts. We aim here to identify the laccase-type oxidoreductases that might be involved in the decolorization of dyes by Leptosphaerulina sp. and to characterize them as potential biotechnological tools.es_ES
dc.description.abstract[Results] A Leptosphaerulina fungal strain, isolated from lignocellulosic material in Colombia, produces laccase as the main ligninolytic oxidoreductase activity during decolorization of synthetic organic dyes. Four laccase-type MCO genes were partially amplified from the genomic DNA using degenerate primers based on laccase-specific signature sequences. The phylogenetic analysis showed the clustering of Lac1, Lac4 and Lac3 with ascomycete laccases, whereas Lac2 grouped with fungal ferroxidases (together with other hypothetical laccases). Lac3, the main laccase produced by Leptosphaerulina sp. in dye decolorizing and laccase-induced cultures (according to the shotgun analysis of both secretomes) was purified and characterized in this study. It is a sensu-stricto laccase able to decolorize synthetic organic dyes with high efficiency particularly in the presence of natural mediator compounds.-
dc.description.abstract[Conclusions] The searching for laccase-type MCOs in ascomycetous families where their presence is poorly known, might provide a source of biocatalysts with potential biotechnological interest and shed light on their role in the fungus. The information provided by the use of genomic and proteomic tools must be combined with the biochemical evaluation of the enzyme to prove its catalytic activity and applicability potential.-
dc.description.sponsorshipThis research was supported by the Program for Interuniversity Cooperation and Scientific Reasearch (PCI) from the Spanish Agency for International Cooperation and Development (AECID), Project AP/033932/11, and the Spanish Project NOESIS BIO2014-56388-R.es_ES
dc.language.isoenges_ES
dc.publisherBioMed Centrales_ES
dc.relationMINECO/ICTI2013-2016/BIO2014-56388-R-
dc.relation.isversionofPublisher's versiones_ES
dc.rightsopenAccesses_ES
dc.subjectLeptosphaerulinaes_ES
dc.subjectMulticopper-oxidaseses_ES
dc.subjectLaccaseses_ES
dc.subjectPhylogenyes_ES
dc.subjectSecretomees_ES
dc.subjectDye decolorizationes_ES
dc.subjectNatural mediatorses_ES
dc.titleIdentification and characterization of laccase-type multicopper oxidases involved in dye-decolorization by the fungus Leptosphaerulina sp.es_ES
dc.typeartículoes_ES
dc.identifier.doi10.1186/s12896-015-0192-2-
dc.description.peerreviewedPeer reviewedes_ES
dc.relation.publisherversionhttp://dx.doi.org/10.1186/s12896-015-0192-2es_ES
dc.identifier.e-issn1472-6750-
dc.rights.licensehttp://creativecommons.org/licenses/by/4.0/es_ES
dc.contributor.funderMinisterio de Asuntos Exteriores y Cooperación (España)-
dc.contributor.funderMinisterio de Economía y Competitividad (España)-
dc.relation.csices_ES
dc.identifier.funderhttp://dx.doi.org/10.13039/501100003767es_ES
dc.identifier.funderhttp://dx.doi.org/10.13039/501100003329es_ES
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