Purification and Properties of D-Xylulose Reductase from Pachysolen tannophilus

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概要

• 論文の詳細を見る

• D-Xylulose reductase (EC 1.1.1.9) from Pachysolen tannophilus IFO 1007 was purified by Sphadex G-100 gel chromatography with three columns and DEAE cellulose chromatography. The purified enzyme was entirely homogenous on disc gel electrophoresis. It was most active at pH 9.1-10.0 and 55℃, and stable at pH 7-9 and below 25℃. Its activity was stimulated by NH_4Cl, NaCl, MgCl_2,KCl, glutathione, cysteine and glycine, and inhibited remarkably by SH inhibitor such as lead acetate, HgCl_2 and AgNO_3. It oxidized xylitol, sorbitol, ribitol and glycerine but not mannitol, inositol, arabitol and erythritol. Its K_m values of enzyme against xylitol, sorbitol and ribitol were 1.1×10^<-2> M, 3.0×10^<-2> M and 5.0×10^<-2> M, respectively. Its molecular weight was determined to be 120,000 by Sephadex G-200 column chromatography, and that of its subunit was 40,000 by sodium dodecyl sulfate polyacrylamide gel electrophoresis.

• 社団法人日本生物工学会の論文
• 1986-06-25

著者

• Sinskey Anthony

  Massachusetts Institute Of Technology

• MORIMOTO SHIGEMI

  Shoin Women's University, Shoin Women's College

• AZUMA KAZUKO

  Shoin Women's University, Shoin Women's College

• Azuma Kazuko

  Shoin Women's University Shoin Women's College

• Morimoto Shigemi

  Shoin Women's University Shoin Women's College

• Morimoto Shigemi

  Shoin Junior College Shoin Women's University

関連論文

• Purification and Properties of Aldose Reductase from Pachysolen tannophilus
• Purification and Properties of D-Xylulose Reductase from Pachysolen tannophilus
• Purification and Properties of a New Enzyme, Propioin Synthase in Baker's Yeast Which Forms Propioin from Propoinaldehyde
• パン酵母によるプロピオンアルデヒドの代謝に関する研究〔英文〕

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