Optimization of enzymatic gas-phase reactions by increasing the long-term stability of the catalyst.

Enzymatic gas-phase reactions are usually performed in continuous reactors, and thus very stable and active catalysts are required to perform such transformations on cost-effective levels. The present work is concerned with the reduction of gaseous acetophenone to enantiomerically pure (R)-1-phenylethanol catalyzed by solid alcohol dehydrogenase from Lactobacillus brevis (LBADH), immobilized onto glass beads. Initially, the catalyst preparation displayed a half-life of 1 day under reaction conditions at 40 degrees C and at a water activity of 0.5. It was shown that the observed decrease in activity is due to a degradation of the enzyme itself (LBADH) and not of the co-immobilized cofactor NADP. By the addition of sucrose to the cell extract before immobilization of the enzyme, the half-life of the catalyst preparation (at 40 degrees C) was increased 40 times. The stabilized catalyst preparation was employed in a continuous gas-phase reactor at different temperatures (25-60 degrees C). At 50 degrees C, a space-time yield of 107 g/L/d was achieved within the first 80 h of continuous reaction.