Journal
BIOTECHNOLOGY LETTERS
Volume 27, Issue 15, Pages 1087-1095Publisher
SPRINGER
DOI: 10.1007/s10529-005-8455-y
Keywords
alcohol dehydrogenase; cofactor regeneration; enzyme deactivation; enzyme kinetics
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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 (k(d)=0.0141 min(-1)) there was no way to keep high conversion of acetophenone at 98%. The deactivation occurred in the repetitive batch as well. A mathematical model for the acetophenone reduction with cofactor regeneration describing the behaviour in a batch, repetitive-batch and continuously stirred tank reactor was developed.
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