Utilize este identificador para referenciar este registo: https://hdl.handle.net/1822/2647

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dc.contributor.authorKandelbauer, A.-
dc.contributor.authorErlacher, Angelika-
dc.contributor.authorPaulo, Artur Cavaco-
dc.date.accessioned2005-08-26T08:43:11Z-
dc.date.available2005-08-26T08:43:11Z-
dc.date.issued2004-12-
dc.identifier.citation"Biocatalysis and biotransformation". ISSN 1024-2422. 22:5-6 (Dec. 2004) 331-339.eng
dc.identifier.issn1024-2422eng
dc.identifier.urihttps://hdl.handle.net/1822/2647-
dc.description.abstractThe kinetics of laccase-catalyzed transformation of the azo-dye Diamond Black PV 200 (CI Mordant Black 9) and various related synthesized derivatives were analyzed for dependence on pH and substrate structure. The reaction mixture of Diamond Black PV 200 was analyzed by HPLC/MS_/MS and it was shown that upon laccase oxidation, reactive chinoid fragments of lower molecular weight were formed. These may further oligomerize as indicated by the appearance of a number of compounds with increased molecular weight. The pH optimum for the decolorization was pH 5 for Diamond Black PV 200 which did not change significantly when the substitution pattern of its basic structure was varied. Biodegradability, however, was strongly dependent on the structure of the dyes.eng
dc.language.isoengeng
dc.publisherTaylor and Franciseng
dc.rightsopenAccesseng
dc.subjectLaccaseeng
dc.subjectAzo-dyeseng
dc.subjectBioremediationeng
dc.subjectEnzyme Kineticseng
dc.subjectSubstrate Specificityeng
dc.subjectDye Transformationeng
dc.titleLaccase-catalyzed decolorization of the synthetic azo-dye diamond black PV 200 and of some structurally related derivativeseng
dc.typearticlepor
dc.peerreviewedyeseng
sdum.publicationstatuspublishedeng
oaire.citationStartPage331por
oaire.citationEndPage339por
oaire.citationIssue5-6por
oaire.citationVolume22por
dc.identifier.doi10.1080/10242420400024573por
dc.subject.wosScience & Technologypor
sdum.journalBiocatalysis and Biotransformationpor
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