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Article: Purification and characterisation of NAD+-dependent xylitol dehydrogenase from Fusarium oxysporum

TitlePurification and characterisation of NAD+-dependent xylitol dehydrogenase from Fusarium oxysporum
Authors
Panagiotou, GKekos, DMacris, BJChristakopoulos, P
KeywordsFusarium Oxysporum
Purification
Xylitol Dehydrogenase
Issue Date2002
PublisherSpringer Verlag Dordrecht. The Journal's web site is located at http://springerlink.metapress.com/openurl.asp?genre=journal&issn=0141-5492
Citation
Biotechnology Letters, 2002, v. 24 n. 24, p. 2089-2092 How to Cite?
DOI: http://dx.doi.org/10.1023/A:1021317614948
AbstractAn NAD+-dependent xylitol dehydrogenase (XDH) from Fusarium oxysporum, a key enzyme in the conversion of xylose to ethanol, was purified to homogeneity and characterised. It was homodimeric with a subunit of Mr 48 000, and pI 3.6. It was optimally active at 45°C and pH 9-10. It was fully stable at pH 6-7 for 24 h and 30°C. Km values for D-xylitol and NAD+ were 94 mM and 0.14 mM, respectively. Mn2+ at 10 mM increased XDH activity 2-fold and Cu2+ at 10 mM inhibited activity completely.
Persistent Identifierhttp://hdl.handle.net/10722/181234
ISSN
0141-5492
2023 Impact Factor: 2.0
2023 SCImago Journal Rankings: 0.519
ISI Accession Number ID
WOS:000179636600012
References
References in Scopus

 

DC FieldValueLanguage
dc.contributor.authorPanagiotou, Gen_US
dc.contributor.authorKekos, Den_US
dc.contributor.authorMacris, BJen_US
dc.contributor.authorChristakopoulos, Pen_US
dc.date.accessioned2013-02-21T02:03:23Z-
dc.date.available2013-02-21T02:03:23Z-
dc.date.issued2002en_US
dc.identifier.citationBiotechnology Letters, 2002, v. 24 n. 24, p. 2089-2092en_US
dc.identifier.issn0141-5492en_US
dc.identifier.urihttp://hdl.handle.net/10722/181234-
dc.description.abstractAn NAD+-dependent xylitol dehydrogenase (XDH) from Fusarium oxysporum, a key enzyme in the conversion of xylose to ethanol, was purified to homogeneity and characterised. It was homodimeric with a subunit of Mr 48 000, and pI 3.6. It was optimally active at 45°C and pH 9-10. It was fully stable at pH 6-7 for 24 h and 30°C. Km values for D-xylitol and NAD+ were 94 mM and 0.14 mM, respectively. Mn2+ at 10 mM increased XDH activity 2-fold and Cu2+ at 10 mM inhibited activity completely.en_US
dc.languageengen_US
dc.publisherSpringer Verlag Dordrecht. The Journal's web site is located at http://springerlink.metapress.com/openurl.asp?genre=journal&issn=0141-5492en_US
dc.relation.ispartofBiotechnology Lettersen_US
dc.subjectFusarium Oxysporumen_US
dc.subjectPurificationen_US
dc.subjectXylitol Dehydrogenaseen_US
dc.titlePurification and characterisation of NAD+-dependent xylitol dehydrogenase from Fusarium oxysporumen_US
dc.typeArticleen_US
dc.identifier.emailPanagiotou, G: gipa@hku.hken_US
dc.identifier.authorityPanagiotou, G=rp01725en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1023/A:1021317614948en_US
dc.identifier.scopuseid_2-s2.0-0036955763en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0036955763&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume24en_US
dc.identifier.issue24en_US
dc.identifier.spage2089en_US
dc.identifier.epage2092en_US
dc.identifier.isiWOS:000179636600012-
dc.publisher.placeNetherlandsen_US
dc.identifier.scopusauthoridPanagiotou, G=8566179700en_US
dc.identifier.scopusauthoridKekos, D=7003932669en_US
dc.identifier.scopusauthoridMacris, BJ=7006746072en_US
dc.identifier.scopusauthoridChristakopoulos, P=7006479823en_US
dc.identifier.issnl0141-5492-

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