PENICILLIUM-PURPUROGENUM PRODUCES SEVERAL XYLANASES - PURIFICATION AND PROPERTIES OF 2 OF THE ENZYMES

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dc.contributor.authorBELANCIC, A
dc.contributor.authorSCARPA, J
dc.contributor.authorPEIRANO, A
dc.contributor.authorDIAZ, R
dc.contributor.authorSTEINER, J
dc.contributor.authorEYZAGUIRRE, J
dc.date.accessioned2025-01-21T01:34:40Z
dc.date.available2025-01-21T01:34:40Z
dc.date.issued1995
dc.description.abstractThe fungus Penicillium purpurogenum produces several extracellular xylanases. The two major forms (xylanases A and B) have been purified and characterized. After ammonium sulfate precipitation and chromatography in Bio-Gel P 100, xylanase A was further purified by means of DEAE-cellulose, hydroxylapatite and CM-Sephadex, and xylanase B by DEAE-cellulose and CM-Sephadex. Both xylanases showed apparent homogeneity in SDS-polyacrylamide gel electrophoresis. Xylanase A (33 kDa) has an isoelectric point of 8.6, while xylanase B (23 kDa) is isoelectric at pH 5.9. Antisera against both enzymes do not cross-react. The amino terminal sequences of xylanases A and B show no homology. The results obtained suggest that the enzymes are produced by separate genes and they may perform different functions in xylan degradation.
dc.fuente.origenWOS
dc.identifier.eissn1873-4863
dc.identifier.issn0168-1656
dc.identifier.urihttps://repositorio.uc.cl/handle/11534/97587
dc.identifier.wosidWOS:A1995RM09500007
dc.issue.numero1
dc.language.isoen
dc.pagina.final79
dc.pagina.inicio71
dc.revistaJournal of biotechnology
dc.rightsacceso restringido
dc.subjectP-PURPUROGENUM
dc.subjectXYLANASE
dc.subjectENZYME PURIFICATION
dc.subjectAMINO ACID SEQUENCE, SIMILARITY
dc.subject.ods12 Responsible Consumption and Production
dc.subject.ods07 Affordable and Clean Energy
dc.subject.odspa12 Producción y consumo responsable
dc.subject.odspa07 Energía asequible y no contaminante
dc.titlePENICILLIUM-PURPUROGENUM PRODUCES SEVERAL XYLANASES - PURIFICATION AND PROPERTIES OF 2 OF THE ENZYMES
dc.typeartículo
dc.volumen41
sipa.indexWOS
sipa.trazabilidadWOS;2025-01-12
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