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  • TBADH activity in water-miscible organic solvents: correlations between enzyme performance, enantioselectivity and protein structure through spectroscopic studies.

TBADH activity in water-miscible organic solvents: correlations between enzyme performance, enantioselectivity and protein structure through spectroscopic studies.

Organic & biomolecular chemistry (2005-02-26)
Linus Olofsson, Ian A Nicholls, Susanne Wikman
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.

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
2-Pentanone, ≥98%, FCC, FG
Sigma-Aldrich
2-Pentanone, ultrapure grade, ≥99.5%
Supelco
2-Pentanone, analytical standard
Sigma-Aldrich
2-Pentanone, reagent grade, ≥90%
Sigma-Aldrich
2-Pentanone, suitable for HPLC, 99.5%