Purification and characterisation of NAD+-dependent xylitol dehydrogenase from Fusarium oxysporum |
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Authors: | G. Panagiotou D. Kekos B.J. Macris P. Christakopoulos |
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Affiliation: | (1) Biotechnology Laboratory, Department of Chemical Engineering, National Technical University of Athens, Zografou Campus, Athens, 157 80, Greece |
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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 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. |
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Keywords: | Fusarium oxysporum purification xylitol dehydrogenase |
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