Immobilization of Kluyvera citrophila penicillins acylase on controlledpore ceramics.

ABSTRACT

Penicillin acylase was purified from Kluyvera citrophila and immobilized on glutaraldehyde derivatives of silanized controlled-pore ceramics. The behaviour of the enzyme attached to TiO2, Al2O3 and SiO2 in the hydrolytic reaction are compared with that of the native enzyme as well as of the enzyme bound to CNBr-activated Sepharose 4B. The enzyme immobilized on TiO2 shows an efficiency of about 95% on the basis of protein bound. The penicillin acylase attached to SiO2, unlike the enzyme immobilized on TiO2, Al2O3 and Sepharose looses activity markedly in every cycle of use.