Stabilization of Enzyme Activity by an Organic Solvent

Abstract

BIOCHEMICAL work with unstable enzymes is often handicapped by the loss of their enzyme activity during preparation and storage, and the instability of the enzymes makes their further purification and study difficult. A number of enzymes can be stabilized with the use of reducing agents, chelating compounds, competitive inhibitors, co-enzymes, and substrates and their analogues. Recently, Nozaki, Kagamiyama and Hayaishi¹ have found that metapyrocatechase from Pseudomonas sp., which is very unstable, particularly in the presence of air, is stabilized by the presence of a low concentration of an organic solvent such as acetone or ethanol, and this observation led to its purification and crystallization. This has led us to investigate whether organic solvents have a stabilizing effect on a wide variety of enzymes. In this communication we report the effects of acetone and ethanol in stabilizing benzylalcohol dehydrogenase from Pseudomonas sp., homogentisicase from bovine liver, and alcohol dehydrogenase from yeast.