Purification and Properties of Beta-Lactamase from Bacteroides fragilis MARGARET L. BRITZ AND RUSSELL G. WILKINSON* School of Microbiology, University of Melbourne, Parkville, Victoria, Australia, 3052 Received for publication 19 August 1978
/8-Lactamase activity was detected either biologically or using the chromogenic cephalosporin 87/312 in 20 clinical isolates of Bacteroides fragilis with penicillin G minimal inhibitory concentrations of 10 to 100 pAg/ml. Strain AM78 (minimal inhibitory concentration, >1,000 ,ug/ml) was used to optimize the conditions for production, assay, and storage of the enzyme. The enzymes are cell associated, with 1,000 3.38 0.190 AM79 B. fragilis subsp. fragilis >1,000 75 0.10 0 B. fragilis AM80 0.50 0.024 225 AM81 B, fragilis 0 25 0.03 AM82 B. fragilis 29.40 8.25 J.53 (RP4) E. coli >1,000 aFor crude broken-cell preparations from ABHI cultures, measured as micromoles hydrolyzed/minute per milligram of protein. b Limits of sensitivity of iodometric assay,