Study on Mesophilic and Thermophilic Alcohol Dehydrogenases in Gas‐Phase Reaction
Study on Mesophilic and Thermophilic Alcohol Dehydrogenases in Gas‐Phase Reaction
复制标题
中温和高温乙醇脱氢酶的气相反应研究
DOI:
10.1021/bp050316g
复制
发表时间:
2006
影响因子:
2.9
通讯作者:
J. Büchs
中科院分区:
文献类型:
--
作者:
A. Trivedi;A. Spiess;T. Daussmann;J. Büchs
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·L−1·d−1 for LBADH and 600 g·L−1·d−1for ADH T was found at 60 °C, while the highest total turnover numbers with respect to the enzyme were achieved at 30 °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.