Utilize este identificador para referenciar este registo: https://hdl.handle.net/1822/58184

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dc.contributor.authorSu, Jingpor
dc.contributor.authorNoro, Jennifer Martinspor
dc.contributor.authorLoureiro, Anapor
dc.contributor.authorMartins, Madalenapor
dc.contributor.authorAzoia, Nuno G.por
dc.contributor.authorFu, Jiajiapor
dc.contributor.authorWang, Qiangpor
dc.contributor.authorSilva, Carla-
dc.contributor.authorCavaco-Paulo, Artur-
dc.date.accessioned2019-01-14T23:01:45Z-
dc.date.available2019-01-14T23:01:45Z-
dc.date.issued2017-10-23-
dc.identifier.citationJing Su; Jennifer Noro; Loureiro, Ana; Martins, Madalena; Fu, Jiajia; Silva, Carla; Cavaco-Paulo, Artur, PEGylation greatly enhances laccase polymerase activity. ChemCatChem, 9(20), 3888-3894, 2017por
dc.identifier.issn1867-3880por
dc.identifier.urihttps://hdl.handle.net/1822/58184-
dc.description.abstractLaccase catalyzes the oxidation and polymerization of phenolic compounds in the presence of oxygen. Herein, we report for the first time that a previous pegylation of laccase enhances the polymerase activity by 3-fold comparing with the native enzyme, as confirmed by UV-Vis spectroscopy. The polymerization of catechol increased only 1.5-fold when polyethyleneglycol (PEG) was added to the medium reaction. Molecular dynamic simulations suggest the formation of a miscible complex of polycatechol and PEG, which is responsible to push the reaction forward. In a negative control experiment set, all catalysts were entrapped inside acrylamide gels and here the native laccase showed a relatively higher activity. These results suggest that the mobility of PEG is a key feature for the enhancement of the reaction.por
dc.description.sponsorshipThis study was supported by Chinese GovernmentScholarship under China Scholarship Council (No. 201606790036), Chinese Foundation Key projects of governmental cooperation in international scientific and technological innovation (No.2 016 YFE0115700), the National Natural Science Foundation of China (No.31470509) and the Fundamental Research Funds for the Central Universities (No.JUSRP51622A). This study was also supported by the Portuguese Foundation for Science and Technology (FCT) under the scope of the strategic funding of UID/BIO/04469/2013 unit and COMPETE2020 (POCI-01–0145-FEDER-006684) and BioTecNorteoperation (NORTE-01–0145-FEDER-000004) fundedb y EuropeanRegional DevelopmentFund under the scope of Norte2020—Programa Operacional Regional do Norte.por
dc.language.isoengpor
dc.publisherWiley-Blackwellpor
dc.relationinfo:eu-repo/grantAgreement/FCT/5876/147337/PTpor
dc.rightsopenAccesspor
dc.subjectlaccasepor
dc.subjectpolyethylene glycolpor
dc.subjectpolymerizationpor
dc.subjecttemplatepor
dc.subjectalcoholspor
dc.subjectenzyme catalysispor
dc.subjectmolecular dynamicspor
dc.subjecttemplate synthesispor
dc.titlePEGylation greatly enhances laccase polymerase activitypor
dc.typearticle-
dc.peerreviewedyespor
dc.relation.publisherversionhttp://onlinelibrary.wiley.com/journal/10.1002/(ISSN)1867-3899por
dc.commentsCEB46915por
oaire.citationStartPage3888por
oaire.citationEndPage3894por
oaire.citationIssue20por
oaire.citationConferencePlaceGermany-
oaire.citationVolume9por
dc.date.updated2019-01-14T17:18:13Z-
dc.identifier.eissn1867-3899por
dc.identifier.doi10.1002/cctc.201700849por
dc.description.publicationversioninfo:eu-repo/semantics/publishedVersionpor
dc.subject.wosScience & Technologypor
sdum.journalChemCatChempor
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