Properties of ß-lactamase from Neisseria gonorrhoeae

ß-lactamase activity was studied in Neisseria gonorrhoeae strains. Optimum temperature was found to be 37ºC. The enzyme was inactivated at temperature higher than 60ºC, but remained active during storage at low temperatures (4ºC, -30ºC and -70ºC) 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 Ni²+, Fe²+, Fe cube number +, Mn²+ and p-chloromercurybenzoate to the reaction buffer exerced a negative effect upon the activity, whereas Hg²+ 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.