Effects of organic solvents on immobilized enzyme catalyses. Chymotrypsin immobilized on porous glass

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Abstract
The esterolytic activity of native chymotrypsin (CT) immobilized on ionically neutral porous glass beads has been studied in the presence of up to 20% (v/v) of the organic solvents methanol, ethanol, 2-propanol, tert-butyl alcohol, dioxane, and DMSO. In marked contrast to the variations observed with native CT, inhibition of CT immobilized on glass (CT–glass) was independent of the nature of the organic solvent. The overall activity, as indicated by kc(app)/km(app), decreased by 35–50% as the concentration of all solvents surveyed was increased up to 20%. In general, high organic solvent concentration accelerated the rate of protein release from the insoluble catalyst. For practical applications in aqueous organic solvents CT–glass conjugates are inferior to those of the enzyme attached to Sephadex.

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