Heterologous expression, purification, and characterization of xylose reductase from Candida shehatae
Heterologous expression, purification, and characterization of xylose reductase from Candida shehatae
复制标题
DOI：
10.1007/s10529-007-9412-8
复制
发表时间：
2007-07
影响因子：
2.7
通讯作者：
Xiaoxia Wang;B. Fang;Juxiang Luo;Wenjun Li;Liaoyuan Zhang
中科院分区：
文献类型：
--
作者：
Xiaoxia Wang;B. Fang;Juxiang Luo;Wenjun Li;Liaoyuan Zhang
从假丝酵母菌中克隆了木糖还原酶(XR)基因(Xyl1)，并在大肠杆菌中表达，纯化为His6标记的融合蛋白。重组XR对NADH的Km值分别为150μM和20μM。最适反应温度为35℃，最适pH为6.5，为福特木聚糖酶。
The xylose reductase (XR) gene (xyl1) fromCandida shehataewas cloned and expressed inEscherichia coli, and purified as a His6-tagged fusion protein. The recombinant XR had Kmvalues for NADH than NADPH of 150 μM and 20 μM, respectively. The optimal reaction was at pH 6.5 and 35°C. The enzyme was specific ford-xylese.