Purification and Properties of the NAD^+-Xylitol-Dehydrogenase from the Yeast Pichia stipitis

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概要

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• 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 electophoretic homogeneity via gel and affinity chromatography. The purified enzyme was most active pH9 and 35℃. Its molecular weighr 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 suphate polyacrylamide gel electrophoresis. From the results of substrate specificity, the emzyme should be named L-iditol : NAD^+-5-oxidoreductase (EC 1.1.1.14,sorbitol dehydrogenase).

• 社団法人日本生物工学会の論文
• 1989-01-25

著者

• Bui-thanh Ngoc-anh

  Institut Fur Biotechnologie Technische University Berlin

• RIZZI MANFRED

  Institut fur Biotechnologie, Technische Universitat Berlin

• HARWART KATHARINA

  Institut fur Biotechnologie, Technische Universitat Berlin

• DELLWEG HANSWERNER

  Institut fur Biotechnologie, Technische Universitat Berlin

• ERLEMANN PETRA

  Institut fur Biotechnologie, Technische University Berlin

• Rizzi M

  Univ. Stuttgart Stuttgart Deu

• Erlemann Petra

  Institut Fur Biotechnologie Technische University Berlin

• Harwart Katharina

  Institut Fur Biotechnologie Technische University Berlin

• Dellweg Hanswerner

  Institut Fur Biotechnologie Technische University Berlin

関連論文

• A Kinetic Study of the NAD^+-Xylitol-Dehydrogenase from the Yeast Pichia stipits
• Purification and Properties of the NAD^+-Xylitol-Dehydrogenase from the Yeast Pichia stipitis
• Screening of Yeasts for Production of Xylitol from D-Xylose

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