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j.bcab.2012.03.003.pdf451.19 kBAdobe PDF見る/開く
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dc.contributor.authorHibi, Makotoen
dc.contributor.authorHatahira, Satokoen
dc.contributor.authorNakatani, Masatoen
dc.contributor.authorYokozeki, Kenzoen
dc.contributor.authorShimizu, Sakayuen
dc.contributor.authorOgawa, Junen
dc.contributor.alternative日比, 慎ja
dc.contributor.alternative小川, 順ja
dc.date.accessioned2012-07-05T01:51:00Z-
dc.date.available2012-07-05T01:51:00Z-
dc.date.issued2012-07-
dc.identifier.issn1878-8181-
dc.identifier.urihttp://hdl.handle.net/2433/157357-
dc.description.abstractExtracellular ligninolytic oxidoreductases produced by Cerrena sp. strain Ra, a soil-isolated basidiomycete with high artificial dye-decolorizing activity, were purified and characterized. One thermostable laccase, one typical manganese peroxidase, and two versatile peroxidases (VPI and VPII) were found in the culture of this fungus. The different characteristics of each enzyme enable the strain express wide-range of oxidizing activity under various conditions. VPI decolorizing activity was observed toward various kinds of dye compounds, and the activity and specificity varied depending on the oxidizing mediators added to the reaction mixture. Optimized VPI/mediator-coupling decolorizing will be widely used for industrial wastewater treatment.en
dc.format.mimetypeapplication/pdf-
dc.language.isoeng-
dc.publisherElsevier Ltd.en
dc.rights© 2012 Elsevier Ltd.en
dc.rightsこの論文は出版社版でありません。引用の際には出版社版をご確認ご利用ください。ja
dc.rightsThis is not the published version. Please cite only the published version.en
dc.subjectVersatile peroxidaseen
dc.subjectDye decolorizationen
dc.subjectCerrena spen
dc.subjectExtracellular oxidoreductaseen
dc.subjectLigninolytic enzymeen
dc.titleExtracellular oxidases of Cerrena sp. complementarily functioning in artificial dye decolorization including laccase, manganese peroxidase, and novel versatile peroxidasesen
dc.typejournal article-
dc.type.niitypeJournal Article-
dc.identifier.jtitleBiocatalysis and Agricultural Biotechnologyen
dc.identifier.volume1-
dc.identifier.issue3-
dc.identifier.spage220-
dc.identifier.epage225-
dc.relation.doi10.1016/j.bcab.2012.03.003-
dc.textversionauthor-
dcterms.accessRightsopen access-
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