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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Bibliographic Details
Published in:Applied microbiology and biotechnology Vol. 29; no. 2/3; pp. 148 - 154
Main Authors: Rizzi, M, Erlemann, P, Bui-Thanh, N.A, Dellweg, H
Format: Journal Article
Language:English
Published: 01-09-1988
Subjects:
enzyme activity
fermentation
isomerization
kinetics
Pichia
purification
xylose
xylose reductase
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Summary: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.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:0175-7598
1432-0614
DOI:10.1007/BF00939299