Abstract
β-Galactosidase from jack bean was immobilized on poly (vinyl alcohol) super fine fibers (SFF) carrying various ionic groups and cation exchangers. Sulfonated SFF (S-SFF) was found to adsorb the enzyme electrostatically much more than aminated SFF and several cation exchangers. S-SFF-β-galactosidase complex (SGC) treated with glutaraldehyde retained the activity for a longer period than that without the treatment. From these results, it is concluded that S-SFF is the excellent support for immobilizing β-galactosidase from jack bean compared with other carriers.
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