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

被引：0
作者：
G. Panagiotou
D. Kekos
B.J. Macris
P. Christakopoulos
机构：
[1] National Technical University of Athens,Biotechnology Laboratory, Department of Chemical Engineering
来源：
Biotechnology Letters | 2002年 / 24卷
关键词：
purification; xylitol dehydrogenase;
D O I：
暂无
中图分类号：
学科分类号：
摘要：
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.
引用
收藏
页码：2089 / 2092
页数：3
相关论文
共 36 条
  • [1] Bolen PL(1986)Affinity purifications of aldose reductase and xylitol dehydrogenase from the xylose fermenting yeast Appl. Environ. Microbiol. 52 660-664
  • [2] Roth KA(1983)The role of redox balances in the anaerobic fermentation of xylose by yeasts Eur. J. Appl. Microbiol. Biotechnol. 18 287-292
  • [3] Freer SN(1960)Metabolism of D-xylose by moulds Nature 188 79-81
  • [4] Bruinenberg PM(1989)Direct fermentation of cellulose to ethanol by Enzyme Microb. Technol. 11 236-239
  • [5] Chiang C(1995)Purification and characterisation of a non-randomly acting endo-1,4- Arch. Biochem. Biophys. 316 428-433
  • [6] Knight SG(1996)-D-glucanase from the culture filtrates of J. Biotechnol. 51 181-189
  • [7] Christakopoulos P(1997)Purification and characterization of two low molecular mass alkaline xylanases from Carbohydr. Res. 302 191-195
  • [8] Kekos D(1994)The alkaline xylanase III from Enzyme Microb. Technol. 16 944-956
  • [9] Macris BJ(1986) belongs to Family F J. Ferment. Technol. 64 219-225
  • [10] Christakopoulos P(1997)Process parameters and environmental factors affecting D-xylose fermentation by yeasts FEMS Lett. 146 79-83
1234