Parasites of the genus Leishmania are transmitted by the bite of sandflies and infect cells of the mononuclear phagocyte lineage of their vertebrate hosts. These parasites can promote a spectrum of diseases known as leishmaniasis. The peptidases are enzymes founded in several organisms, since virus until human. They are involved in a large scale of biological reactions, such as protein metabolism, immune response and blood coagulation. These enzymes seem to be involved with a range of vital activities of parasites, as virulence, nutrition and escape mechanisms. In this work, we have compared the pattern of peptidases in two strains of Leishmania braziliensis: an infective and non-infective one. The presence of E-64 (cysteine peptidase inhibitor), EGTA and phenanthroline (metallopeptidase inhibitors) drastically inhibited the cell growth of infective strain, while in the non-infective strain these inhibitors had no effect. These inhibitors also promoted a decrease on the association index between Leishmania infective strain and macrophage. EGTA, phenantroline and E-64 inhibited 31.05%, 35.40% and 42.57% this process, respectively. After extraction, the peptidases founded in cytoplasmic content were separated in gelatin-SDS-PAGE. The profile presented by infective and non-infective promastigote forms were distinct. The infective parasites presented a pronounced peptidase activity  (40, 49, 60 and 80 kDa) in acid pH (5,5), while in non-infective strain, this activity was lower (60 kDa). EGTA and phenantroline inhibited peptidase activity presented by 60 and 80 kDa, while E-64 inihibited peptidase activity presented by 40 and 49 kDa. These enzymes seem to be related with important process such as cell growth and infectivity.