Improvement of the enzyme immobilisation characteristics of macroporous cellulose trans-2,3-carbonate by pre-swelling in dimethyl sulphoxide

Abstract

The amount of chymotrypsin A protein covalently bound to macroporous cellulose trans-2,3-carbonate and the caseinolytic activity of the resulting immobilised enzyme have been substantially improved by swelling the matrix in dimethyl sulphoxide before coupling with the enzyme. This improvement has been attributed to an increase in the porosity of the insoluble support during the pre-swelling process which enables macromolecules to diffuse into the matrix. Storage of the cellulose carbonate under inappropriate conditions before coupling with protein resulted in an irreversible deterioration in the physical characteristics of the matrix.