CHARACTERISTICS OF IMMOBILIZED BETA-GALACTOSIDASE FROM CICER-ARIETINUM

Sephadex G-100 modified with chloroacetic acid and CEAH was prepared i nto cationic and anionic carriers and activated by CNBr. beta-Galactos idase I (beta-D-galactoside galactohydrolase EC 3.2.1.23) isolated and partially purified from gram chicken bean was immobilized on modified Sephadex G-100 by means of adsorption and crosslinking reaction. Both the anionic and cationic gel carriers have high protein binding capac ity and high yield of enzyme activity. Kinetic results showed that the enzyme activity attained its maximum at 57 degrees C for cationic car riers and 52 degrees C for anionic carriers. In addition, the operatio nal pH range of the immobilized enzyme was increased. Storage stabilit y of the immobilized enzyme preparations at room temperature was bette r than that of soluble enzyme. Results of the repeated batch experimen ts suggested that immobilized enzymes could be reused.