Inducible oxacillin-hydrolyzing penicillinase in Aeromonas hydrophila isolated from fish

Abstract

An inducible penicillinase was shown to be present in a strain of Aeromonas hydrophila subsp. hydrophila isolated from freshwater fish. Enzyme induction was observed with benzylpenicillin or 6-aminopenicillanic acid, and the enzyme was cell bound. The penicillinase was purified 50-fold from a crude cell extract. The molecular weight was estimated to be 23,000 by gel filtration. The pH and temperature optima for the enzyme activity were 8.0 and 35 degrees C, respectively. The penicillinase showed a unique substrate profile by hydrolyzing oxacillin about twice as rapidly as benzylpenicillin. The enzyme activity was weakly inhibited by sodium chloride but was not affected by p-chloromercuribenzoate. The property of penicillinase production by the A. hydrophila strain could not be transferred to Escherichia coli and also could not be eliminated from the bacteria by ethidium bromide treatment.