Purification and characterization of xylitol dehydrogenase from Fusarium oxysporum

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

doi:10.1023/A:1021317614948

Purification and characterization of xylitol dehydrogenase from Fusarium oxysporum

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

Research output: Contribution to journal › Journal article › Research › peer-review

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 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 language	English
Journal	Biotechnology Letters
Volume	24
Issue number	24
Pages (from-to)	2089-2092
ISSN	0141-5492
DOIs	https://doi.org/10.1023/A:1021317614948
Publication status	Published - 2002

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@article{08cfbaed1d284881b9c26ee7732db6e9,

title = "Purification and characterization of xylitol dehydrogenase from Fusarium oxysporum",

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 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.",

author = "Gianni Panagiotou and D. Kekos and B.J. Macris and Paul Christakopoulos",

year = "2002",

doi = "10.1023/A:1021317614948",

language = "English",

volume = "24",

pages = "2089--2092",

journal = "Biotechnology Letters",

issn = "0141-5492",

publisher = "Springer Science and Business Media B.V.",

number = "24",

}

TY - JOUR

T1 - Purification and characterization of xylitol dehydrogenase from Fusarium oxysporum

AU - Panagiotou, Gianni

AU - Kekos, D.

AU - Macris, B.J.

AU - Christakopoulos, Paul

PY - 2002

Y1 - 2002

N2 - 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.

AB - 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.

U2 - 10.1023/A:1021317614948

DO - 10.1023/A:1021317614948

M3 - Journal article

SN - 0141-5492

VL - 24

SP - 2089

EP - 2092

JO - Biotechnology Letters

JF - Biotechnology Letters

IS - 24

ER -

Purification and characterization of xylitol dehydrogenase from Fusarium oxysporum

Abstract

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