Archana H. Trivedi, Antje Spieß, Thomas Daussmann, Jochen Büchs:
Study on mesophilic and thermophilic alcohol dehydrogenases in gas-phase reaction
Biotechnology Progress, 2006, 22(2), 454-458
The initial reaction rate and the thermostability of the mesophilic alcohol dehydrogenase (ADH) from Lactobacillus brevis (LBADH), and the thermophilic ADH from Thermoanaerobacter sp. (ADH T) in gas-phase reaction were compared. The effects of water activity, cofactor-to-protein molar ratio, and reaction temperature on the reduction of acetophenone to 1-phenylethanol were studied. An optimal water activity of 0.55 in terms of productivity was found for both ADHs. The cofactor-to-protein molar ratio was chosen slightly higher than equimolar to increase both activity and thermostability. An excellent optimal productivity of 1000 g center dot L-1 center dot d(-1) for LBADH and 600 g center dot L-1 center dot d(-1) for ADH T was found at 60 degrees C, while the highest total turnover numbers with respect to the enzyme were achieved at 30 degrees C and amounted to 4.2 million for LBADH and 1.7 million for ADH T, respectively. Interestingly, the ADH from the mesophilic L. brevis showed the higher thermostability in the nonconventional medium gas phase.