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A novel protease with fibrinolytic activity was purified from MucorsubtilissimusUCP 1262usinga two-step purification protocol.The enzyme was pre-purified using cetonic precipitation and adsorbed by ion exchange chromatography on DEAE-sephadex G50. System two-dimensional electrophoresis (2DE) coupled to SDS-PAGE showed a single protein band of15.3kDa approximatelyand isoeletric focusing point of 3.9, exhibiting a nature as an acidic enzyme.The activity was suppressed by Co 2+ and HgCl2, but slightly enhanced byCa 2+ . Additionally, the activity was slightly inhibited by EDTA, but significantlyinhibited by PMSF. It exhibited fibrinolytic activity,which is weaker than that of plasmin, but also had a higher affinity for the N-Succinyl-Ala-Ala-Pro-Phe p-nitroanilide (SAAPNA) and azocasein substrates, suggesting a chymotrypsin-like protease. These results demonstrated an economically viable protocol purification of a protease with fibrinolytic activity with high degree of purity that may represent a potential source of new therapeutic agents to treat thrombosis.

PURIFICATION AND CHARACTERIZATION OF A NOVEL PROTEASE WITH FIBRINOLYTIC ACTIVITY FROM Mucor subtilissimus UCP 1262