Beta-lactamase activity was studied in Neisseria gonorrhoeae
strains. Optimum temperature was found to be 37 C. The enzyme was
inactivated at temperatures higher than 60 C, but remained active during
storage at low temperatures (4 C, -30 C and -70 C) for two months. Enzyme
activity was observed within a pH range of 5.8-8.0, while the optimum pH
was 7.0-7.2. Addition of Ni^2+, Fe^2+, Fe^3+, Mn^2+ and
p-chloromercurybenzoate to the reaction buffer exerted a negative effect
upon the activity, whereas Hg^2+ and ethylene diamine tetra-acetic acid
produced complete inhibition. These results would indicate the presence of
-SH groups at the catalytic site of the enzyme.
