Oxalate oxidase from <i>Ceriporiopsis subvermispora</i>

dc.contributor.authorAguilar, C
dc.contributor.authorUrzúa, U
dc.contributor.authorKoenig, C
dc.contributor.authorVicuña, R
dc.date.accessioned2025-01-21T01:32:01Z
dc.date.available2025-01-21T01:32:01Z
dc.date.issued1999
dc.description.abstractThe enzyme oxalate oxidase was identified in mycelial extracts of the basidiomycete Ceriporiopsis subvermispora and thereafter purified to homogeneity. The purification procedure included only three steps: Q-Sepharose chromatography, precipitation at pH 3.0, and phosphocellulose chromatography. The enzyme is a 400-kDa homohexamer, as determined by gel permeation in Sephadex G-200 and SDS-polyacrylamide gel electrophoresis. Isoelectrofocusing revealed a pi of 4.2. Optimal activity was obtained at pH 3.5 and at 45 degrees C. The purified enzyme has K-m and k(cat) values of 0.1 mM and 88 s(-1), respectively. It is highly specific for oxalate, although it is inhibited at concentrations of this substrate above 2.5 mM. Hystochemistry studies conducted over mycelium slices showed reactions products in both endocellular and periplasmic associated elements. A possible connection between the intracellular metabolism of oxalate and the extracellular ligninolytic activity of the fungus is proposed. (C) 1999 Academic Press.
dc.fuente.origenWOS
dc.identifier.eissn1096-0384
dc.identifier.issn0003-9861
dc.identifier.urihttps://repositorio.uc.cl/handle/11534/97189
dc.identifier.wosidWOS:000080904800013
dc.issue.numero2
dc.language.isoen
dc.pagina.final282
dc.pagina.inicio275
dc.revistaArchives of biochemistry and biophysics
dc.rightsacceso restringido
dc.subjectoxalate oxidase
dc.subjectoxalic acid
dc.subjecthydrogen peroxide
dc.subjectCeriporiopsis subvermispora
dc.subject.ods06 Clean Water and Sanitation
dc.subject.odspa06 Agua limpia y saneamiento
dc.titleOxalate oxidase from <i>Ceriporiopsis subvermispora</i>
dc.typeartículo
dc.volumen366
sipa.indexWOS
sipa.trazabilidadWOS;2025-01-12
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