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Viable cells, cell free extracts and extracellular concentrates of Micrococcus roseus (65), Halomonas elongata (16) and Vibrio sp. (168) isolated from Danish bacon curing brines were examined for lipase, esterase, proteinase and aminopeptidase activities on natural and synthetic substrates. Micrococcus roseus (65) produced one intracellular esterase with affinity for short chain esters, and two intracellular aminopeptidases with affinity for nonpolar amino acids and L-arginine, respectively. One extracellular aminopeptidase with affinity for L-proline was also observed. Three intracellular esterases with affinity for short chain esters and a membrane bound esterase with affinity for butyric to capric esters were found in Halomonas elongata (16), but almost no aminopeptidase activity was found. Vibrio sp. (168) had four intracellular esterases with affinity for short chain esters and one esterase with affinity for all tested esters. Furthermore, an enzyme, which did not migrate on electrophoretic gels, had activity on all examined esters and tributyrin. Small intracellular activity on L-alanine was observed for this bacterial strain. There was no proteinase activities in the tested bacteria.