ABSTRACT

Trypsin was immobilized onto alumina (AI,O,) by the adsorption. The immobilized enzyme showed higher catalytic activities than free enzyme for amino acid peptidation. Studies of the kinetics of peptide synthesis catalyzed by trypsin have been carried out. We have studied on and prepared the trypsin derivatives with the enhanced stabilities and have used these successfully for initial dipeptide synthesis. We have studied on the equilibrium controlled synthesis(ECS) by using benzoyl arginine and leucinamide as substrates and mainly tested a number of variables, e.g. the temperature and pH. Optimal experimental conditions for that synthetic approach was established in order to simultaneously obtain good values for all industrial parameters.