Kinetic Modeling of Acetophenone Reduction Catalyzed by Alcohol Dehydrogenase from Thermoanaerobacter sp.

@article{Findrik2005KineticMO,
  title={Kinetic Modeling of Acetophenone Reduction Catalyzed by Alcohol Dehydrogenase from Thermoanaerobacter sp.},
  author={Zvjezdana Findrik and Đurđa Vasic’-Ra{\vc}ki and Stephan Luetz and Thomas Daussmann and Christian Wandrey},
  journal={Biotechnology Letters},
  year={2005},
  volume={27},
  pages={1087-1095}
}
NADPH-dependent alcohol dehydrogenase (ADH) from Thermoanaerobacter sp. was kinetically characterized using reduction of acetophenone as a model. To achieve 98% conversion of acetophenone, cofactor regeneration by oxidation of 2-propanol with the same enzyme was used. The enzyme was stable in the batch reactor. It was enantioselective towards (S)-1-phenylethanol (ee>99.5%). Due to its high deactivation in continuously operated stirred tank reactor (kd=0.0141 min−1) there was no way to keep high… CONTINUE READING

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