Immobilization of Kluyvera citrophila penicillins acylase on controlled-pore 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.