Abstract
CRUDE preparations of penicillinase from Bacillus cereus N.R.R.L. 569, unlike the purified penicillinase from this organism or crude penicillinase from Staphylococcus aureus R1, have been shown to catalyse the hydrolysis of the β-lactam ring of cephalosporin C and other derivatives of 7-aminocephalosporanic acid at a significant rate. The enzyme responsible for this hydrolysis was termed a cephalosporinase1,2. The maximum rate of hydrolysis (Vmax) of cephalosporin C obtained with a crude enzyme from B. cereus was only 5 per cent of that of benzyl-penicillin, but this value increased to 33 per cent after selective inactivation of penicillinase in aqueous solution at 60° C. Subsequent studies were made with a crude enzyme from Bacillus subtilis N.C.T.C. 6346, induced with cephalosporin C and freed from the cells by the action of lysozyme3. With this enzyme preparation Vmax for cephalosporin C was about 10 per cent that for benzyl-penicillin, but attempts to separate a cephalosporinase from a penicillinase, or selectively inactivate a penicillinase, were unsuccessful.
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