THE HYDROLYSIS OF PENICILLIN G TO 6-AMINO PENICILLANIC ACID BY ENTRAPPED PENICILLIN ACYLASE

Abstract

Penicillin acylase was extracted from Escherichia coli strain ATCC 9637, purified and entrapped in celluose triacetate fibres. The enzyme was immobilized by trapping it, as a finely dispersed aqueous phase, in yarns of cellulose triacetate by wet spinning. The kinetics of penicillin G hydrolysis were studied by use of several insoluble preparations with different activity content. In an attempt to evaluate the possible industrial application of the process, the performance of an entrapped acylase reactor was investigated.