Isoenzyme multiplicity and characterization of recombinant manganese peroxidases from <i>Ceriporiopsis subvermispora</i> and <i>Phanerochaete chrysosporium</i>

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dc.contributor.authorLarrondo, LF
dc.contributor.authorLobos, S
dc.contributor.authorStewart, P
dc.contributor.authorCullen, D
dc.contributor.authorVicuña, R
dc.date.accessioned2025-01-21T01:30:53Z
dc.date.available2025-01-21T01:30:53Z
dc.date.issued2001
dc.description.abstractWe expressed cDNAs coding for manganese peroxidases (MnPs! from the basidiomycetes Ceriporiopsis subvermispora (MnP1) and Phanerochaete chrysosporium (H4) under control of the alpha -amylase promoter from. Aspergillus oryzae in Aspergillus nidulans. The recombinant proteins (rMnP1 and rH4) were expressed at similar Levels and had molecular masses, both before and after deglycosylation, that were the same as those described For the MnPs isolated from the corresponding parental strains. Isoelectric focusing (IEF) analysis of rH4 revealed several isoforms with pls between 4.83 and 4.06, and one of these pls coincided with the pi described for H4 isolated from P. chrysosporium (pl 4.6). IEF of rMnP1 resolved four isoenzymes with pIs between 3.45 and 3.15, and the pattern closely resembled the pattern observed with MnPs isolated from C. subvermispora grown in solid-state cultures. We compared the abilities of recombinant MnPs to use various substrates and found that rH4 could oxidize o-dianisidine and p-anisidine without externally added manganese, a property not previously reported for this MnP isoenzyme from P. chrysosporium.
dc.fuente.origenWOS
dc.identifier.issn0099-2240
dc.identifier.urihttps://repositorio.uc.cl/handle/11534/96922
dc.identifier.wosidWOS:000168488400012
dc.issue.numero5
dc.language.isoen
dc.pagina.final2075
dc.pagina.inicio2070
dc.revistaApplied and environmental microbiology
dc.rightsacceso restringido
dc.subject.ods06 Clean Water and Sanitation
dc.subject.odspa06 Agua limpia y saneamiento
dc.titleIsoenzyme multiplicity and characterization of recombinant manganese peroxidases from <i>Ceriporiopsis subvermispora</i> and <i>Phanerochaete chrysosporium</i>
dc.typeartículo
dc.volumen67
sipa.indexWOS
sipa.trazabilidadWOS;2025-01-12
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