PURIFICATION, CHARACTERIZATION, AND AMINO TERMINAL SEQUENCE OF XYLOSE REDUCTASE FROM CANDIDA-SHEHATAE

被引：41

作者：

HO, NWY ^{[1
]}

LIN, FP ^{[1
]}

HUANG, S ^{[1
]}

ANDREWS, PC ^{[1
]}

TSAO, GT ^{[1
]}

机构：

[1] PURDUE UNIV,DEPT BIOCHEM,W LAFAYETTE,IN 47907

来源：

ENZYME AND MICROBIAL TECHNOLOGY | 1990年 / 12卷 / 01期

基金：

美国国家科学基金会;

关键词：

14;

D O I：

10.1016/0141-0229(90)90177-R

中图分类号：

Q81 [生物工程学（生物技术）]; Q93 [微生物学];

学科分类号：

071005 ; 0836 ; 090102 ; 100705 ;

摘要：

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. © 1990.

引用

页码：33 / 39

页数：7

共 14 条

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[2] AFFINITY PURIFICATIONS OF ALDOSE REDUCTASE AND XYLITOL DEHYDROGENASE FROM THE XYLOSE-FERMENTING YEAST PACHYSOLEN-TANNOPHILUS [J].