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 45 °C and pH 9–10. It was fully stable at pH 6–7 for 24 h and 30 °C. 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.
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Panagiotou, G., Kekos, D., Macris, B. et al. Purification and characterisation of NAD+-dependent xylitol dehydrogenase from Fusarium oxysporum . Biotechnology Letters 24, 2089–2092 (2002). https://doi.org/10.1023/A:1021317614948
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DOI: https://doi.org/10.1023/A:1021317614948