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

Panagiotou, G; Kekos, D; Macris, BJ; Christakopoulos, P

dc.contributor.author	Panagiotou, G	en
dc.contributor.author	Kekos, D	en
dc.contributor.author	Macris, BJ	en
dc.contributor.author	Christakopoulos, P	en
dc.date.accessioned	2014-03-01T01:18:16Z
dc.date.available	2014-03-01T01:18:16Z
dc.date.issued	2002	en
dc.identifier.issn	0141-5492	en
dc.identifier.uri	https://dspace.lib.ntua.gr/xmlui/handle/123456789/14901
dc.subject	Fusarium oxysporum	en
dc.subject	Purification	en
dc.subject	Xylitol dehydrogenase	en
dc.subject.classification	Biotechnology & Applied Microbiology	en
dc.subject.other	Fusarium	en
dc.subject.other	Fusarium oxysporum	en
dc.title	Purification and characterisation of NAD+-dependent xylitol dehydrogenase from Fusarium oxysporum	en
heal.type	journalArticle	en
heal.identifier.primary	10.1023/A:1021317614948	en
heal.identifier.secondary	http://dx.doi.org/10.1023/A:1021317614948	en
heal.language	English	en
heal.publicationDate	2002	en
heal.abstract	An 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 M-r 48 000, and pI 3.6. It was optimally active at 45degreesC and pH 9-10. It was fully stable at pH 6-7 for 24 h and 30degreesC. K-m 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
heal.publisher	KLUWER ACADEMIC PUBL	en
heal.journalName	Biotechnology Letters	en
dc.identifier.doi	10.1023/A:1021317614948	en
dc.identifier.isi	ISI:000179636600012	en
dc.identifier.volume	24	en
dc.identifier.issue	24	en
dc.identifier.spage	2089	en
dc.identifier.epage	2092	en