Purification and properties of d-xylulose reductase from Pachysolen tannophilus |
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| Affiliation: | 1. Shoin Women''s University, Shoin Women''s College, 1-2-1 Shinohara Obanayamacho, Nadaku-ku, Kobe 657, Japan;1. Shoin Women''s University, Shoin Women''s College, Part-time Lecturer, Japan;7. Massachusetts Institute of Technology, Cambridge, Massachusetts, U.S.A.;1. Drilling Technology Laboratory (DTL), Faculty of Engineering and Applied Science, Memorial University of Newfoundland, St. John''s, NL, A1B 3X5, Canada;2. Hibernia Enhanced Oil Recovery Group (EOR), Faculty of Engineering and Applied Science, Memorial University of Newfoundland, St. John''s, NL, A1B 3X5, Canada;3. Centre for Risk, Integrity and Safety Engineering (CRISE), Faculty of Engineering and Applied Science, Memorial University of Newfoundland, St. John''s, NL, A1B 3X5, Canada;1. Electrodics & Electrocatalysis Division, CSIR-Central Electrochemical Research Institute (CECRI), Karaikudi, Tamil Nadu, 630003, India;2. Academy of Scientific and Innovative Research (AcSIR)-CSIR, Ghaziabad, Uttar Pradesh, 201002, India;3. Amity Institute of Biotechnology, Amity University, Jaipur, Rajasthan, 303002, India |
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| Abstract: | d-Xylulose reductase (EC 1.1.1.9) from Pachysolen tannophilus IFO 1007 was purified by Sephadex G-100 gel chromatography with three columns and DEAE cellulose chromatography. The purified enzyme was entirely homogeneous on disc gel electrophoresis. It was most active at pH 9.1–10.0 and 55°C, and stable at pH 7–9 and below 25 °C. Its activity was stimulated by NH4Cl,NaCl,MgCl2,KCl, glutathione, cysteine and glycine, and inhibited remarkably by SH inhibitor such as lead acetate, HgCl2 and AgNO3. It oxidized xylitol, sorbitol, ribitol and glycerine but not mannitol, inositol, arabitol and erythritol. Its Km 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. |
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