Purification of a stereospecific 2-ketoreductase from Gluconobacter oxydans |
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| Authors: | V B Nanduri A Banerjee J M Howell D B Brzozowski R F Eiring R N Patel |
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| Affiliation: | (1) Enzyme Technology, Process Research, Bristol-Myers Squibb Pharmaceutical Research Institute, P.O. Box 191, New Brunswick, NJ 08903 , |
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| Abstract: | The 2-ketoreductase from Gluconobacter oxydans (SC 13851) catalyzes the reduction of 2-pentanone to (S)-(+)-2-pentanol. The 2-ketoreductase was purified 295-fold to homogeneity from G. oxydans cell extracts. The purified 2-ketoreductase had a molecular mass of 29 kDa with a specific activity of 17.7 U/mg. (S)-(+)-2-pentanol was prepared on a pilot scale (3.2 kg of 2-pentanone input) using Triton X-100-treated G. oxydans cells. After 46 h, 1.06 kg (32.3 M%) of (S)-(+)-2-pentanol of >99% enantiomeric excess (ee) was produced. Journal of Industrial Microbiology & Biotechnology (2000) 25, 171–175. Received 01 May 2000/ Accepted in revised form 28 June 2000 |
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| Keywords: | : Gluconobacter oxydans (S)-(+)-2-pentanol 2-ketoreductase enzyme purification |
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