The localization of hydrolytic enzymes, phosphatase, estcrase, lipase and palmitoyl-CoA hydrolase was analysed in the cytosol, cytoplasmic membrane, periplasmic fraction, outer membrane and culture supernatant in dependence on the growth rate of the bacteria.
The unspecific phosphatase was found to be a cytosolic enzyme.
A lipase was the only extracellular enzyme detected. The results pointed to a secretion of the lipase into the culture medium via cytoplasmic and outer membrane.
The palmitoyl-CoA hydrolase was found to be attached to the outer membrane, but activities were also detected in the periplasmic fraction.
Unspecific esterolytic activities were mainly measured in the cytosol and in the cytoplasmic membrane.
Hydrolases are common enzymes in microorganisms. Lipolytic (BAUMANN et al. 1968) and esterolytic activities (BREUIL and KUSHNER 1975) are known to be present in species of Acinetobacter. HAFERBURG and KLEBER (1982, 1983) and KOSLOWSKI (1981) detected also a lipase and esterase in A . calcoaceticus. The cellular localization and the growth dependence of which remained, however, to be elucidated.
Results concernig these enzymes should be compared with the palmitoyl-CoA hydrolase found as an outer membrane protein (CLAUS et al. 1985) and the phosphatase from A . calcoaceticus.
This paper deals with the localization of the hydrolytic enzyme lipase, esterase, phosphatase and palmitoyl-CoA hydrolase in the cytosol, cytoplasmic membrane, periplasmic fraction, outer membrane and culture supernatant and the distinction of these enzymes from each other with respect to their place of function.