Purification and characterization of xylitol dehydrogenase from Fusarium oxysporum

Gianni Panagiotou, D. Kekos, B.J. Macris, Paul Christakopoulos

    Research output: Contribution to journalJournal articleResearchpeer-review


    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.
    Original languageEnglish
    JournalBiotechnology Letters
    Issue number24
    Pages (from-to)2089-2092
    Publication statusPublished - 2002


    Dive into the research topics of 'Purification and characterization of xylitol dehydrogenase from Fusarium oxysporum'. Together they form a unique fingerprint.

    Cite this