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Purification, characterization, and amino terminal sequence of xylose reductase fromCandida shehatae

Authors
Journal
Enzyme and Microbial Technology
0141-0229
Publisher
Elsevier
Publication Date
Volume
12
Issue
1
Identifiers
DOI: 10.1016/0141-0229(90)90177-r
Disciplines
  • Agricultural Science
  • Biology

Abstract

Abstract d- Xylose is a major component of the carbohydrates derived from agricultural residues and forest products. Among more than two hundred known xylose-utilizing yeasts, only a few species are known to be able to ferment xylose anaerobically. Candida shehatae is one of such xylose-fermenting yeasts. Xylose reductase (E.C. 1.1.1.21) is a key enzyme responsible for xylose metabolism in xylose-utilizing as well as xylose-fermenting yeasts. In this paper, we report the development of a convenient and reliable procedure for the purification of xylose reductase from C. shehatae to near homogeneity. The amino acid composition and N-terminal sequence of the enzyme have also been analyzed. C. shehatae seems to contain only a single xylose reductase, but the enzyme has a dual coenzyme specificity for both NADPH and NADH. The enzyme is remarkably stable at room temperature and 4°C.

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