Utilize este identificador para referenciar este registo: https://hdl.handle.net/1822/2626

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Campo DCValorIdioma
dc.contributor.authorZille, Andrea-
dc.contributor.authorMunteanu, Florentina-Daniela-
dc.contributor.authorGübitz, Georg M.-
dc.contributor.authorPaulo, Artur Cavaco-
dc.date.accessioned2005-08-24T16:17:58Z-
dc.date.available2005-08-24T16:17:58Z-
dc.date.issued2005-
dc.identifier.citation"Journal of molecular catalysis B: enzymatic". ISSN 1381-1177. 33 (2005). 23-28eng
dc.identifier.issn1381-1177eng
dc.identifier.urihttps://hdl.handle.net/1822/2626-
dc.description.abstractThe ability of Trametes villosa laccase to degrade an azo dye (methyl orange) and to catalyze the coupling reactions between the aromatic amines and catechol was studied. It was found that the apparent Michaelis–Menten constants obtained from amperometric measurements were comparable to the ones obtained in the oxygen consumption experiments (8.20 and 7.40 µM, respectively). From the measurements of the mediated and mediatorless currents of azo dye degradation and coupling reactions itwas concluded that the addition of 1-hydroxybenzotriazole (HBT) as mediator considerably improves the catalytic efficiencies. It can be concluded that the mediated coupling of the aromatic amine with catechol opens the perspectives of physical removal of these polluting chemicals from the nature and the usage of the laccase immobilized onto macro-electrodes in online systems with continuous monitoring of the enzyme activity.eng
dc.language.isoengeng
dc.publisherElsevier 1eng
dc.rightsopenAccesseng
dc.subjectKineticseng
dc.subjectLaccaseeng
dc.subjectAzo dyeeng
dc.subjectCouplingeng
dc.subjectAromatic amineseng
dc.titleLaccase kinetics of degradation and coupling reactionseng
dc.typearticlepor
dc.peerreviewedyeseng
sdum.publicationstatuspublishedeng
oaire.citationStartPage23por
oaire.citationEndPage28por
oaire.citationIssue1-2por
oaire.citationVolume33por
dc.identifier.doi10.1016/j.molcatb.2005.01.005por
dc.subject.wosScience & Technologypor
sdum.journalJournal of Molecular Catalysis B: Enzymaticpor
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