| Abstract: | Peptidase activity determinations involving native cells of Streptococcus cremoris and completely disrupted cell preparations, as well as experiments concerned with peptidase activity distribution among cell fractions obtained by a damage-restrictive removal of the cell wall and release of intracellular material, suggest the presence of peptidases with distinguishable locations. Alanyl, leucyl, and prolyl aminopeptidase activities are most likely located in the cell wall-membrane interface, showing no detectable association with the membrane. Lysyl aminopeptidase is present not only in this location, but also as an intracellular enzyme. Endopeptidase activity and glutamate aminopeptidase activity appear to be weakly associated with the membrane. The locations of these two peptidase activities, unlike those of the former aminopeptidase activities, impose a restriction on their expression. Results of experiments concerned with permeabilization of the membrane and findings regarding an effect of the local environment of the enzymes on their pH activity profiles are evaluated and considered as being indicative of the proposed location. The possible implications of these findings with respect to protein utilization during growth of the organism in milk are discussed. |
