Serine metalloprotease with plasmin-like fibrinolytic activity of Serratia marcescens isolated from the Amazon basin

Research on new fibrinolytic agents has been oriented towards the discovery of microbial proteases with plasmin-like activity, as alternative thrombolytic for thrombosis treatment. This study reports characterization an extracellular serine metalloprotease approximately 56 kDa, and fibrinogenolytic isolated from a S. marcescens strain obtained Amazon (CBAM 519). The enzyme showed optimum activity at pH 9 temperature 37 °C. Activity was reduced in presence Na+, Cu2+ Fe2+ ions, increased Mn2⁺. did not show hemolytic nor it activate plasminogen, but effectively hydrolyzed fibrin fibrinogen, rapidly degrading all fibrinogen chains Aα, Bβ γ. Therefore, fibrinolysis promoted only by direct route, fast acting, potent activity. Based this, we expect to be protease plasmin type that directly degrades fibrin. These characteristics demonstrate great potential its application treatment thrombosis.