Preparation and properties of proteases immobilized on anion exchange resin with glutaraldehyde

High activity alkaline protease was obtained when the enzyme was immobilized on Dowex MWA-1 (mesh 20-50) with 10% glutaraldehyde in chilled phosphate buffer (M/15, PH 6.5). Activity yields of the protease and rennet were 27 and 29, respectively. The highest activities appeared at 60 degrees C, pH 10 for alkaline protease and 50 degrees C, pH 4.0 for rennet. The properties of both proteases were not essentially changed by the immobilization except that the Km values of both enzymes were increased about tenfold as a result of immobilization. Both proteases in the immobilized state were more stable than those in the free state at 60 degrees C. Other peptide hydrolases, beta-galactosidase, invertase, and glucoamylase, were successfully immobilized with high activities, but lipase, hexokinase, glucose-6-phosphate dehydrogenase, and xanthine oxidase became inactive.