alpha-chymotrypsin and cellulose-triacetate

Immobilization of alpha-chymotrypsin on carboxymethyl esters of dextran (mol. weights of 60 000 and 100 000), whose macromolecules contain 2-amino-4-chloro-s-triazine residues, results in water-soluble polymeric derivatives of alpha-chymotrypsin, containing up to 60% of the enzyme. The activity of the immobilized enzyme makes up to 90% of the initial one. Using dextran blue as a matrix, a polymeric derivative of alpha-chymotrypsin, containing 9% of a chemically bound enzyme, which retains 20% of its initial activity, has been obtained in a similar way. The thermal stability of the enzyme increases during alpha-chymotrypsin linking to carmoxymethyl esters of dextran. The incorporation of alpha-chymotrypsin into the triacetate cellulose membrane (CTA) during its formation results in a practically complete desorption of the enzyme from the membrane into 1 M NaCl. During incorporation of alpha-chymotrypsin linked to the carboxymethyl ester of dextran (mol. weight 60 000) into the CTA membrane the bulk of the modified enzyme is desorbed, whereas in the case of alpha-chymotrypsin linked to the carboxymethyl ester of dextran with mol. weight of 100 000 or to the blue dextran only an insignificant part of the enzyme is desorbed. The thermal stability of alpha-chymotrypsin and the labile form of the enzyme linked to the carboxymethyl ester of dextran with mol. weight of 100 000 increases during the enzyme incorporation into the CTA membrane.

Topics: Cellulose; Chymotrypsin; Enzymes, Immobilized; Kinetics; Molecular Weight