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Updated: Aug 19, 2026

Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes
Published on: January 16, 2016
TBADH activity in water-miscible organic solvents: correlations between enzyme performance, enantioselectivity and
Linus Olofsson1, Ian A Nicholls, Susanne Wikman
1Bioorganic & Biophysical Chemistry Laboratory, Department of Chemistry & Biomedical Sciences, University of Kalmar, SE-391 82, Kalmar, Sweden. linus.olofsson@hik.se
Abstract:
The enantioselective reduction of 2-pentanone to (R)- and (S)-2-pentanol by Thermoanaerobacter (formerly Thermoanaerobium) brockii alcohol dehydrogenase (TBADH) in mixtures of water and water-miscible organic solvents was investigated. Significant enzymatic activity was retained in up to 87% methanol, ethanol and acetonitrile. The changes in enzyme activity as a function of organic solvent were correlated to structural alterations of TBADH with a series of spectroscopic studies (fluorescence, fluorescence quenching and circular dichroism (CD)). Interestingly, this study shows that the tetrameric form of TBADH is not critical for catalytic performance.
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