| STUDY |
Enzymes would be more widely used in organic solvents if their activity were not so drastically reduced. That has prompted author to look for ways to enhance the activity of certain enzymes in nonaqueous media. They find that four lyophilized oxidative enzymes--horseradish peroxidase, soybean peroxidase, Caldariomyces fumago chloroperoxidase, and mushroom polyphenol oxidase--function better in nonaqueous media if they are introduced by first dissolving them in water and then diluting the solution with anhydrous solvents. The enzymes, which are denatured during lyophilization, exhibit very little activity when suspended directly in a nonaqueous medium. But they reactivate if first redissolved in water. Author also suggest two complementary ways to minimize or eliminate enzyme inactivation due to lyophilization: use of phenolic and aniline substrates to protect the hydrophobic pocket of the active site and prevent its collapse, and use of protectants such as polyols and polyethylene glycol to preserve the overall enzyme structure.
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