IMMOBILIZATION OF PENICILLIN-G ACYLASE ON AMINOALKYLATED POLYACRYLIC SUPPORTS

A procedure is described for the immobilization of penicillin G acylas e (PA) on Amberline XAD7 modified by transamidation with 1,2-ethylened iamine and activated with glutaraldehyde. Reduction with sodium borohy dride of the Schiff's bases formed between the amino groups of the pro tein and glutaraldehyde results in a dramatic improvement of the opera tional stability of the immobilized enzyme without affecting the catal ytic activity. The enzyme kept in presence of the substrate, penicilli n G, displays an increased stability with respect to that stored in pu re phosphate buffer solution. The inactivation kinetics of the immobil ized preparations of PA, determined in a continuous fixed bed reactor, as well as a discontinuous batch reactor, are reported.