Purification and properties of the NAD+-xylitol-dehydrogenase from the yeast Pichia stipitis |
| |
Institution: | 1. College of Mechanical and Electronic Engineering, Northwest A & F University, Yangling, Shaanxi 712100, China;2. College of Food Science and Pharmacy, Xinjiang Agricultural University, Urumqi, Xinjiang 830052, China;3. College of Food Science and Engineering, Northwest A & F University, Yangling, Shaanxi 712100, China |
| |
Abstract: | Cell-free extracts of the xylose fermenting yeast Pichia stipitis exhibited xylitol dehydrogenase activity with NAD+ and NADP+. During the purification step on DEAE-sephadex A-50 a NAD+-dependent xylitol dehydrogenase could be separated from a NADP+-dependent. The NAD+-xylitol dehydrogenase was further purified to electrophoretic homogeneity via gel and affinity chromatography. The purified enzyme was most active at pH 9 and 35°C. Its molecular weight was determined to be 63,000 dalton by Sephadex G-200 column chromatography, and that of its subunit was 32,000 dalton by sodium dodecyl sulphate polyacrylamide gel electrophoresis. From the results of substrate specificity, the enzyme should be named l-iditol:NAD+-5-oxidoreductase (EC 1.1.1.14, sorbitol dehydrogenase). |
| |
Keywords: | |
本文献已被 ScienceDirect 等数据库收录! |
|