Study on mesophilic and thermophilic alcohol dehydrogenases in gas-phase reaction.
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 1,000 g x L(-1) x d(-1) for LBADH and 600 g x L(-1) x 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. brevisshowed the higher thermostability in the nonconventional medium gas phase.
Trivedi
Archana H
AH
Biochemical Engineering, RWTH Aachen University, Worringerweg 1, D-52056 Aachen, Germany.
Spiess
Antje C
AC
Daussmann
Thomas
T
Büchs
Jochen
J
D000426:Alcohol Dehydrogenase / Q000378:metabolism*; D004795:Enzyme Stability; D004800:Enzymes, Immobilized / Q000378:metabolism; D052196:Levilactobacillus brevis / Q000201:enzymology; D044367:Phase Transition; D013696:Temperature; D046968:Thermoanaerobacter / Q000201:enzymology; D014867:Water
D004800:Enzymes, Immobilized; D014867:Water; D000426:Alcohol Dehydrogenase