Get access

Bioreductions Catalyzed by an Alcohol Dehydrogenase in Non-aqueous Media

Authors

  • Dr. Selin Kara,

    Corresponding author
    1. Institute of Microbiology, Chair of Molecular Biotechnology, Technische Universität Dresden, 01062 Dresden (Germany), Fax: (+49) 0351-463-39520
    2. Department of Biotechnology, Biocatalysis Group, Delft University of Technology, Julianalaan 136, 2628 BL Delft (The Netherlands), Fax: (+31) 015-278-1415
    • Selin Kara, Institute of Microbiology, Chair of Molecular Biotechnology, Technische Universität Dresden, 01062 Dresden (Germany), Fax: (+49) 0351-463-39520

      Frank Hollmann, Department of Biotechnology, Biocatalysis Group, Delft University of Technology, Julianalaan 136, 2628 BL Delft (The Netherlands), Fax: (+31) 015-278-1415

    Search for more papers by this author
  • Dominik Spickermann,

    1. evocatal GmbH, Alfred-Nobel-Str. 10, 40789 Monheim am Rhein (Germany)
    Search for more papers by this author
  • Dr. Andrea Weckbecker,

    1. evocatal GmbH, Alfred-Nobel-Str. 10, 40789 Monheim am Rhein (Germany)
    Search for more papers by this author
  • Dr. Christian Leggewie,

    1. evocatal GmbH, Alfred-Nobel-Str. 10, 40789 Monheim am Rhein (Germany)
    Search for more papers by this author
  • Prof. Dr. Isabel W. C. E. Arends,

    1. Department of Biotechnology, Biocatalysis Group, Delft University of Technology, Julianalaan 136, 2628 BL Delft (The Netherlands), Fax: (+31) 015-278-1415
    Search for more papers by this author
  • Dr. Frank Hollmann

    Corresponding author
    1. Department of Biotechnology, Biocatalysis Group, Delft University of Technology, Julianalaan 136, 2628 BL Delft (The Netherlands), Fax: (+31) 015-278-1415
    • Selin Kara, Institute of Microbiology, Chair of Molecular Biotechnology, Technische Universität Dresden, 01062 Dresden (Germany), Fax: (+49) 0351-463-39520

      Frank Hollmann, Department of Biotechnology, Biocatalysis Group, Delft University of Technology, Julianalaan 136, 2628 BL Delft (The Netherlands), Fax: (+31) 015-278-1415

    Search for more papers by this author

Abstract

Highly productive biocatalytic reductions were established using an isolated alcohol dehydrogenase (ADH) under water-deficient conditions. First, a solvent-free system was evaluated for the reduction of 2-butanone catalyzed by ADH evo-1.1.200 promoted by the “smart cosubstrate” 1,4-butanediol. ADH evo-1.1.200 excelled by its activity and stability under high reagent concentrations and hence was the enzyme of choice. However, conversion of 2-butanone was limited to <1 % in 10 days under the solvent-free conditions. Therefore, water-immiscible organic solvents were evaluated whereby the highest conversions were achieved in MTBE and toluene. MTBE was chosen as its different boiling point compared to other reaction components (e.g., 2-butanone, 2-butanol, diol cosubstrate, and lactone coproduct) would simplify the downstream processing. Further on, by tuning substrate loading, the productivity of the ADH evo-1.1.200 was successfully increased to a turnover number (TON) of 64 000.

Ancillary