Abstract
The degree of substitution of macroporous cellulose withtrans-2,3-cyclic carbonate groups has been controlled by moderating the reaction with water. Exercise of this control enabled the preparation of a matrix with physical and chemical properties which facilitated the covalent binding of chymotrypsin A in such a way that the activity of the insoluble enzyme was appreciable towards a high molecular weight substrate (casein) as well as towards a low molecular weight substrate (tyrosine ethyl ester). Under the optimum conditions of preparation the bound protein had a relative activity towards casein of 26% and towards the ester of 65% of the activity of the free enzyme.
Published Version
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