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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Acetonitriles / chemistry
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Acrylamide / chemistry
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Alcohol Dehydrogenase / chemistry*
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Alcohol Dehydrogenase / isolation & purification
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Circular Dichroism
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Ethanol / chemistry
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Methanol / chemistry
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Oxidation-Reduction
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Pentanones / chemistry
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Protein Conformation
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Protein Structure, Quaternary
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Protein Structure, Secondary
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Protein Subunits / chemistry
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Spectrometry, Fluorescence
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Stereoisomerism
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Thermoanaerobacter / enzymology*
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Tryptophan / chemistry
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Water / chemistry*
Substances
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Acetonitriles
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Pentanones
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Protein Subunits
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Water
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Acrylamide
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Ethanol
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Tryptophan
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Alcohol Dehydrogenase
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2-pentanone
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Methanol
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acetonitrile