Abstract
β-galactosidase from E. Coli was immobilized on three kinds of poly (vinyl alcohol) super fine fibers (SFF) carrying a different functional group. Dimethylaminated SFF (D-SFF) and trimethylaminated SFF (T-SFF) were found to adsorb the enzyme much more than sulfonated SFF (S-SFF). Optimum pH, optimum temperature, and thermal stability of the enzyme were negligibly affected by immobilization. β-galactosidase from E. Coli immobilized on D-SFF retained the activity for a longer period than the enzyme from jack bean bound on S-SFF. D-SFF is found to be the excellent support for immobilizing β-galactosidase from E. Coli and is expected to be applied to a continuous enzymatic reactor.
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