α-Chymotrypsin Immobilized on Chitin. Relationships Between the Enzyme Kinetic Constant and Support Structure

Abstract

α-Chymotrypsin was immobilized on chitin from squills, lobsters and prawns by means of glutaraldehyde. Hydrolase and peptide synthetase activities were determined in aqueous and homogeneous aqueous-organic media, respectively.

The results show α-chymotrypsin immobilized on chitin from prawn to be the most active immobilized derivative based on its synthetase activity (90% yield of Bz-Tyr-Leu-NH₂ in carbonate buffer, p^H 9 containing 70% 1,4- butanediol).

The relationship between the kinetic constant of hydrolysis and chitin structure was also studied. α-Chymotrypsin immobilized on prawn chitin was found to be the best derivative in kinetic terms.

The stability of the three derivatives was studied at 37d`C.

Key Words:

• Chitin
• α-chymotrypsin
• kinetic parameters