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-proteinmolar ratio, and reaction temperature on the reduction of acetophenone to 1-phenylethanol werestudied. 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 bothactivity and thermostability. An excellent optimal productivity of 1000 g·L
-1·d
-1 for LBADHand 600 g·L
-1·d
-1for ADH T was found at 60
C, while the highest total turnover numberswith respect to the enzyme were achieved at 30
C and amounted to 4.2 million for LBADHand 1.7 million for ADH T, respectively. Interestingly, the ADH from the mesophilic
L. brevisshowed the higher thermostability in the nonconventional medium gas phase.