It has been presumed that there are just two beta-lactamases in the mo
tile Aeromonas species, a carbapenemase and a cephalosporinase, based
on the premise that all beta-lactamases can be detected by hydrolysis
of the chromogenic cephalosporin, nitrocefin. However, when it was rec
ently found that a non-motile species of Aeromonas that causes furuncu
losis in salmon, contained three beta-lactamases, one of which was a c
arbapenemase which could not be detected with nitrocefin, it was hypot
hesised that genetic exchange could occur between fish pathogens and h
uman pathogens resulting in the transfer of the carbapenemase-encoding
gene. This could have a potentially serious impact on intensive thera
py units where carbapenems are employed. The purpose of this study was
to determine whether the human pathogen Aeromonas hydrophila demonstr
ated the same beta-lactamase profile. After anion and cation exchange
chromatography had been employed to separate the beta-lactamases of a
clinical strain of A. hydrophila, three different beta-lactamases were
found, one of which is a carbapenemase which does not hydrolyse nitro
cefin. It is, therefore, probable that many strains of Aeromonas spp.
contain a similar array of beta-lactamases which include a carbapenema
se that cannot be detected with nitrocefin. Similar carbapenemases may
well remain hidden in other species of bacteria unless appropriate te
chniques to detect the enzymes are employed.