THE EFFECT OF PH ON THE KINETICS OF PENICILLIN-G ACYLASE OBTAINED FROM A MUTANT OF ESCHERICHIA-COLI ATCC-11105

The competitive inhibition of pH on the kinetics of penicillin G (Pen G) hydrolysis by penicillin G acylase (PGA) obtained from a mutant derivative of Escherichia coli ATCC 11105 was investigated The effect of pH on the initial reaction rate was interpreted according to a mechanism discussed by Tippon and Dixon. Molecular dissociation constants pK(B)E and pK(B)ES of PGA were calculated to be 9.783 and 10.851 respectively.