NADPH-dependent D-aldose reductases and xylose fermentation in Fusarium oxysporum

Gianni Panagiotou, P. Christakopoulos

    Research output: Contribution to journalJournal articleResearchpeer-review


    Two aldose (xylose) reductases (ARI and ARII) from Fusarium oxysporum were purified and characterized. The native ARI was a monomer with M-r 41000, pI 5.2 and showed a 52-fold preference for NADPH over NADH, while ARII was homodimeric with a subunit of M-r 37000, pI 3.6 and a 60-fold preference for NADPH over NADH. In this study, the influence of aeration and the response to the addition of electron acceptors on xylose fermentation by F. oxysporum were also studied. The batch cultivation of F. oxysporum on xylose was performed under aerobic, anaerobic and oxygen-limited conditions in stirred tank reactors. Oxygen limitation had considerable influence on xylose metabolism. Under anaerobic conditions (0 vvm), xylitol was the main product with a maximum yield of 0.34 mole of xylitol/mole of xylose while the maximum ethanol yield (1.02 moles of ethanol/mole of xylose) was obtained under aerobic conditions (0.3 vvm). When the artificial electron acceptor acetoin was added to an anaerobic batch fermentation of xylose by F. oxysporum, the ethanol yield increased while xylitol excretion was also decreased.
    Original languageEnglish
    JournalJournal of Bioscience and Bioengineering
    Issue number5
    Pages (from-to)299-304
    Publication statusPublished - 2004


    Dive into the research topics of 'NADPH-dependent D-aldose reductases and xylose fermentation in Fusarium oxysporum'. Together they form a unique fingerprint.

    Cite this