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J. Biol. Chem., Vol. 263, Issue 17, 8017-8021, Jun, 1988
A Zaks and AM Klibanov
Three model, unrelated enzymes (yeast alcohol oxidase, mushroom polyphenol
oxidase, and horse liver alcohol dehydrogenase) were found to be
catalytically active in a variety of organic solvents. For all enzymes and
solvents tested, the enzymatic activity greatly increased upon an increase
in the water content in the solvents (which always remained below the
solubility limit). Much less water was required to reach the maximal
activity in hydrophobic solvents than in their hydrophilic counterparts.
However, when the catalytic activity was plotted versus the amount of water
bound to the enzymes, a common pattern emerged for different solvents.
These data suggest that the effect of organic solvents on an enzyme is
primarily due to interactions with the enzyme-bound, essential layer of
water rather than with the enzyme itself. At optimal water contents,
enzymatic activities in organic solvents were in the range from 20 to 40%
of those in aqueous solutions. From experiments on (i) replacement of water
with other hydrogen bond-forming additives and (ii) titration of enzyme
amino groups in an organic medium, as well as the literature data on
dehydrated enzymes, it is concluded that the water required by enzymes in
nonaqueous solvents provides them with sufficient conformational
flexibility needed for catalysis.
The effect of water on enzyme action in organic media
Department of Applied Biological Sciences, Massachusetts Institute of Technology, Cambridge 02139.
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