engleski

Kinetic modeling of acetophenone reduction catalyzed by alcohol dehydrogenase from Thermoanaerobacter sp.

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 showed to be highly 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 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.

alcohol dehydrogenase ; cofactor regeneration ; enzyme deactivation ; enzyme kinetics

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