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dc.contributor.authorMaté, Diana M.-
dc.contributor.authorGarcía-Burgos, Carlos-
dc.contributor.authorGarcía-Ruiz, Eva-
dc.contributor.authorBallesteros Olmo, Antonio-
dc.contributor.authorCamarero, Susana-
dc.contributor.authorAlcalde Galeote, Miguel-
dc.date.accessioned2012-02-29T12:33:50Z-
dc.date.available2012-02-29T12:33:50Z-
dc.date.issued2010-09-24-
dc.identifier.citationChemistry and Biology 17(9) : 1030-1041 (2010)es_ES
dc.identifier.issn1074-5521-
dc.identifier.urihttp://hdl.handle.net/10261/46385-
dc.description12 páginas, 5 figuras, 2 tablas -- PAGS nros. 1030-1041es_ES
dc.description.abstractThermostable laccases with a high-redox potential have been engineered through a strategy that combines directed evolution with rational approaches. The original laccase signal sequence was replaced by the α-factor prepro-leader, and the corresponding fusion gene was targeted for joint laboratory evolution with the aim of improving kinetics and secretion by Saccharomyces cerevisiae, while retaining high thermostability. After eight rounds of molecular evolution, the total laccase activity was enhanced 34,000-fold culminating in the OB-1 mutant as the last variant of the evolution process, a highly active and stable enzyme in terms of temperature, pH range, and organic cosolvents. Mutations in the hydrophobic core of the evolved α-factor prepro-leader enhanced functional expression, whereas some mutations in the mature protein improved its catalytic capacities by altering the interactions with the surrounding residueses_ES
dc.description.sponsorshipEU Projects (NMP4-SL-2009-229255, NMP2-CT-2006-026456, COST Action CM0701) and National projects (CTQ2005-08925-CO2-02, BIO2010-19697 and CCG08-CSIC/PPQ-3706). NeuronBiopharma for financial support through Research Contracts 020401070029 (Profit Program) and 020401070004 (Idea Program).-
dc.language.isoenges_ES
dc.publisherElsevieres_ES
dc.relationinfo:eu-repo/grantAgreement/EC/FP7/229255-
dc.relation.isversionofPostprint-
dc.rightsopenAccesses_ES
dc.subjectLacassees_ES
dc.subjectChemistryes_ES
dc.subjectDirected Molecular Evolutionses_ES
dc.subjectEnzymologyes_ES
dc.subjectGeneticses_ES
dc.subjectMetabolismes_ES
dc.subjectOxidation Reduction Reactiones_ES
dc.subjectpHes_ES
dc.subjectProtein Stabilityes_ES
dc.subjectProtein Tertiary Structurees_ES
dc.subjectSaccharomyces Cerevisaees_ES
dc.subjectSite Directed Mutagenesises_ES
dc.titleLaboratory Evolution of High-Redox Potential Laccaseses_ES
dc.typeartículoes_ES
dc.identifier.doi10.1016/j.chembiol.2010.07.010-
dc.description.peerreviewedPeer reviewedes_ES
dc.relation.publisherversionhttp://dx.doi.org/10.1016/j.chembiol.2010.07.010-
dc.identifier.e-issn1879-1301-
dc.contributor.funderEuropean Commission-
dc.contributor.funderNeuron Biopharma-
dc.contributor.funderMinisterio de Economía y Competitividad (España)-
dc.identifier.funderhttp://dx.doi.org/10.13039/501100000780es_ES
dc.identifier.funderhttp://dx.doi.org/10.13039/501100003329es_ES
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