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dc.contributor.authorSerrano, Anaes_ES
dc.contributor.authorSancho, Ferránes_ES
dc.contributor.authorViña-González, Javieres_ES
dc.contributor.authorCarro, Juanes_ES
dc.contributor.authorAlcalde Galeote, Migueles_ES
dc.contributor.authorGuallar, Victores_ES
dc.contributor.authorMartínez, Ángel T.es_ES
dc.date.accessioned2019-01-31T13:52:05Z-
dc.date.available2019-01-31T13:52:05Z-
dc.date.issued2019-01-22-
dc.identifier.citationCatalysis Science & Technology (2019)es_ES
dc.identifier.issn2044-4753-
dc.identifier.urihttp://hdl.handle.net/10261/175056-
dc.description9 p.-8 fig.-4 tab.es_ES
dc.description.abstractOxidation of primary alcohols by aryl-alcohol oxidase (AAO), a flavoenzyme that provides H2O2 to fungal peroxidases for lignin degradation in nature, is achieved by concerted hydroxyl proton transfer and stereoselective hydride abstraction from the pro-R benzylic position. In racemic secondary alcohols, the R-hydrogen abstraction would result in the selective oxidation of the S-enantiomer to the corresponding ketone. This stereoselectivity of AAO may be exploited for enzymatic deracemization of chiral mixtures and isolation of R-enantiomers of industrial interest by switching the enzyme activity from primary to secondary alcohols. A combination of computational simulations and mutagenesis has been used to produce AAO variants with increased activity on secondary alcohols, using the already available F501A variant of Pleurotus eryngii AAO as a starting point. Adaptive-PELE simulations for the diffusion of (S)-1-(p-methoxyphenyl)-ethanol in this variant allowed Ile500 to be identified as one of the key residues with a higher number of contacts with the substrate during its transition from the solvent to the active site. Substitution of Ile500 produced more efficient variants for the oxidation of several secondary alcohols, and the I500M/F501W double variant was able to fully oxidize (after 75 min) with high selectivity (ee >99%) the S-enantiomer of the model secondary aryl-alcohol (±)-1-(p-methoxyphenyl)-ethanol, while the R-enantiomer remained unreacted.es_ES
dc.description.sponsorshipThis work was supported by the INDOX ( KBBE-2013-7-613549) EU project and by the BIO2017-86559-R (GenoBioref), CTQ2016-79138-R and BIO2016-79106-R projects of the Spanish Ministry of Economy, Industry and Competitiveness, cofinanced by FEDER funds.es_ES
dc.language.isoenges_ES
dc.publisherRoyal Society of Chemistry (Great Britain)es_ES
dc.relationinfo:eu-repo/grantAgreement/EC/FP7/613549es_ES
dc.relationMICIU/ICTI2017-2021/BIO2017-86559-Res_ES
dc.relationMINECO/ICTI2013-2016/CTQ2016-79138-Res_ES
dc.relationMINECO/ICTI2013-2016/BIO2016-79106-Res_ES
dc.relation.isversionofPublisher's versiones_ES
dc.rightsopenAccesses_ES
dc.titleSwitching the substrate preference of fungal arylalcohol oxidase: towards stereoselective oxidation of secondary benzyl alcoholses_ES
dc.typeArtículoes_ES
dc.identifier.doi10.1039/C8CY02447b-
dc.description.peerreviewedPeer reviewedes_ES
dc.relation.publisherversionhttps://doi.org/10.1039/C8CY02447bes_ES
dc.identifier.e-issn2044-4761-
dc.rights.licensehttps://creativecommons.org/licenses/by-nc/3.0/es_ES
dc.contributor.funderMinisterio de Economía, Industria y Competitividad (España)es_ES
dc.contributor.funderEuropean Commissiones_ES
dc.relation.csices_ES
oprm.item.hasRevisionno ko 0 false*
dc.identifier.funderhttp://dx.doi.org/10.13039/501100000780es_ES
dc.contributor.orcidCarro, Juan [0000-0002-7556-9782]es_ES
dc.contributor.orcidAlcalde Galeote, Miguel [0000-0001-6780-7616]es_ES
dc.contributor.orcidGuallar, Victor [0000-0002-4580-1114]es_ES
dc.contributor.orcidMartínez, Ángel T. [0000-0002-1584-2863]es_ES
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