IMMOBILIZATION AND CHARACTERISTICS OF BETA-GALACTOSIDASE ON POLYMER RESIN

Sephadex G-100 modified with chloracetic acid and CEAH was prepared in to cationic and anionic carriers and actived by CNBr. beta-galactosida se (beta-D-galactoside galacto hydrolase EC3.2.1.23) isolated and part ially purified from gram chicken bean was immobilized on modified Seph adex G-100 by means of adsorption of ions and crosslinked reaction. Bo th the anionic and cationic gel carriers have high protein binding cap acity and high yield of enzyme activity. Kinetic results showed that t he enzyme activity attained its maximum at 57 degrees C for cationic c arriers and 52 degrees C for anionic carriers. In addition, the operat ional pH range of the immobilized preparations were increased. The imm obilized enzymes showed good storage stability at room temperature tha n that of soluble enzyme. Results of repeated batch experiment suggest ed that the immobilized enzymes could be reused.