Abstract
The performance (activity, stability, enantioselectivity and productivity) of the commercial ketoreductase immobilized on non-porous glass supports was investigated as functions of the water activity and the reaction temperature in a continuous gas phase reactor. The enantioselective reduction of 2-butanone to ( S)-2-butanol with the in situ regeneration of β-nicotinamide adenine dinucleotide phosphate by 2-propanol catalyzed by the immobilized ketoreductase was used as a model reaction. The activity, stability and enantioselectivity were strongly influenced by the water activity and the reaction temperature. The optimal water activity and reaction temperature were obtained at 0.8 and 313–323 K in terms of the productivity, respectively. Successfully, the enantioselectivity for the gas phase system attained the level identical to that for the aqueous phase system.
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