Studies on Immobilized Trypsin in High Concentrations of Organic Solvents

Abstract

It is well known that the rate of enzymic reactions involving ions or dipolar molecules can be modified or effected by the ionic strength of the reaction medium. It has also been shown that the addition of organic solvents to the reaction medium can also change the reaction rates of enzymes (1,2). Recent studies by Royer (3) have indicated that if trypsin is immobilized on control pore glass in the presence of BAEE, several changes occur in the kinetic parameters of the immobilized enzyme. We have attempted in this study to extend the observations of Royer in aqueous systems to systems containing high concentrations of organic solvents of differing dielectric constant and to determine the effect of these solvents on the activity of the immobilized trypsin.