Xylose fermentation by yeasts. 4. Purification and kinetic studies of xylose reductase from Pichia stipitis

Xylose fermentation by yeasts. 4. Purification and kinetic studies of xylose reductase from Pichia stipitis

Xylose reductase from the xylose-fermenting yeast Pichia stipitis was purified to electrophoretic homogeneity via ion-exchange, gel and affinity chromatography. At physiological pH values the thermodynamic equilibrium constant was determined to be 0.575 x 10(10) (1.mol-1). Product inhibition studies...

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Veröffentlicht in:Applied microbiology and biotechnology 1988-09, Vol.29 (2/3), p.148-154
Hauptverfasser: Rizzi, M, Erlemann, P, Bui-Thanh, N.A, Dellweg, H
Format: Artikel
Sprache:eng
Schlagworte:
enzyme activity
fermentation
isomerization
kinetics
Pichia
purification
xylose
xylose reductase
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Zusammenfassung:Xylose reductase from the xylose-fermenting yeast Pichia stipitis was purified to electrophoretic homogeneity via ion-exchange, gel and affinity chromatography. At physiological pH values the thermodynamic equilibrium constant was determined to be 0.575 x 10(10) (1.mol-1). Product inhibition studies are reported which clearly show that the kinetic mechanism of the xylose reductase is ordered-bi-bi with isomerisation of a stable enzyme form.
ISSN:0175-7598
1432-0614
DOI:10.1007/BF00939299