A number of application for enzymes in organic solvents have been developed in chemical processing, food related conversions and analyses. The only unsolved problem related to nonaqueous enzymology is the notion that enzymes in organic solvent are mostly far less active than in water. Therefore, studies concerning the mechanisms by which enzymes are inactivated by organic solvents would reveal a clear understanding of the structure-function relationship of this phenomenon. Here we analyzed the effects of a series of alcohols (methanol, ethanol, 1-propanol and 2-propanol) and acetone on the activity of yeast inorganic pyrophosphatase. We observed that solvents inactivated the enzyme in a dose-dependent manner. This inactivation is also dependent on the... |