CONICET | Buscador de Institutos y Recursos Humanos

Fungal fibrinolytic enzymes, secreted by some Agaricomycetes, are recognized asimportant thrombolytic agents due to their ability to rapidly dissolve thromboembolicclots. Thus the current research focuses on bioprospecting fungal fibrinolytic enzymeswith biotechnological applications in the medical field. The present work evaluatedproteolytic and fibrinolytic secretion abilities of 35 Agaricomycete isolates from theParanaense rainforest (Misiones, Argentina). Proteolytic and fibrinolytic activities weredetermined on skimmilk agar plates and fibrin agarose plates, respectively. Wedetected proteolytic activity in about 40% of the strains while nine strains showedfibrinolytic activity. Schizophyllum commune LBM 026, Schizophyllum communeLBM 223, and Hornodermoporus martius LBM 224 strains exhibited the highest levelsof fibrinolytic activity. Fibrin zymography enzymes from S. commune LBM 026 and S.commune LBM 223 showed a similar band profile with a single enzyme of 27.5 kDa,while H. martius LBM 224 presented a single enzyme of 29 kDa. The evaluation ofthe enzymatic stability of the culture supernatant of S. commune LBM 026 and S.commune LBM 223, revealed that the fibrinolytic activity was highly stable rangingfrom 20?37 C and in the pH range 3.6 to 6.7 for 1 h, while H. martius LBM 224retained its activity in the ranging from 20?37 C and in the pH range 3.6 to 9. Longterm stability of fibrinolytic activity of the culture supernatants at physiologicalconditions evidenced that the strains had a halflife of at least 72 h. Fibrinolytic enzymesproduced by S. commune LBM 026 and S. commune LBM 223 were inhibited in thepresence of EDTA indicating that they are metalloproteases. This work reveals thepotential of S. commune LBM 026, S. commune LBM 223, and H. martius LBM 224strains as an unconventional source of thrombolytic agents

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