One-step purification of Actinoplanes missouriensis -xylose isomerase by high-performance immobilized copper-affinity chromatography: Functional analysis of surface histidine residues by site-directed mutagenesis

One-step purification of Actinoplanes missouriensis -xylose isomerase by high-performance immobilized copper-affinity chromatography: Functional analysis of surface histidine residues by site-directed mutagenesis

D-Xylose isomerase (XI) is a heat-stable homotetrameric enzyme used in industry for the production of high-fructose corn syrups by isomerization of D-glucose into D-fructose. To carry out biochemical and structural studies of this enzyme and of its engineered variants, a rapid and convenient method...

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Bibliographic Details
Published in:Biochemistry (Easton) Vol. 31; no. 10; pp. 2690 - 2702
Main Author: Mrabet, N T
Format: Journal Article
Language:English
Published: 01-01-1992
Subjects:
Actinoplanes missouriensis
activity
histidine
requirements
xylose isomerase
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Summary:D-Xylose isomerase (XI) is a heat-stable homotetrameric enzyme used in industry for the production of high-fructose corn syrups by isomerization of D-glucose into D-fructose. To carry out biochemical and structural studies of this enzyme and of its engineered variants, a rapid and convenient method of purification of recombinant Actinoplanes missouriensis XI produced in Escherichia coli has been developed.
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ISSN:0006-2960