Utilize este identificador para referenciar este registo: https://hdl.handle.net/1822/21897

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Campo DCValorIdioma
dc.contributor.authorSilva, Maria Cristina-
dc.contributor.authorCorrêa, Angelita D.-
dc.contributor.authorAmorim, M. T. Pessoa de-
dc.contributor.authorParpot, Pier-
dc.contributor.authorTorres, Juliana A.-
dc.contributor.authorChagas, Pricila Maria Batista-
dc.date.accessioned2012-12-20T14:31:55Z-
dc.date.available2012-12-20T14:31:55Z-
dc.date.issued2012-
dc.date.submitted2012-
dc.identifier.issn1381-1177por
dc.identifier.urihttps://hdl.handle.net/1822/21897-
dc.description.abstractPeroxidases can be used in decolorization processes and the treatment of textiles effluents. This study evaluates the potential of the turnip peroxidase enzyme in the decolorization of the phthalocyanine textile dye Reactive Blue 21 (RB21). Some factors such as pH, the amount of H2O2 and the enzyme were evaluated in order to determine the optimum conditions for the enzyme performance. The reaction products formed during the decolorization of the RB21 dye were analyzed by high-performance liquid chromatography–mass spectrometry coupling (LC–ESI/MS). LC–ESI/MS analysis showed that the decolorization of the dye RB21 by turnip peroxidase is due to the breaking up of the chromatogenous system. The tests for toxicity towards lettuce seeds showed an increase of the toxicity after enzymatic treatment of the dye. This study verifies the viability of the use of the turnip peroxidase enzyme in the biodegradation of textile dyes.por
dc.description.sponsorshipFAPEMIGpor
dc.description.sponsorshipCNPqpor
dc.description.sponsorshipCAPESpor
dc.language.isoengpor
dc.publisherElsevier 1por
dc.rightsopenAccesspor
dc.subjectEnvironmental biocatalysispor
dc.subjectLC–ESI/MSpor
dc.subjectTurnip peroxidasepor
dc.subjectDecolorizationpor
dc.subjectTextile dyespor
dc.titleDecolorization of the phthalocyanine dye reactive blue 21 by turnip peroxidase and assessment of its oxidation productspor
dc.typearticlepor
dc.peerreviewedyespor
sdum.publicationstatuspublishedpor
oaire.citationStartPage9por
oaire.citationEndPage14por
oaire.citationVolume77por
dc.identifier.doi10.1016/j.molcatb.2011.12.006por
dc.subject.wosScience & Technologypor
sdum.journalJournal of Molecular Catalysis B: Enzymaticpor
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