Production and Stability of the Proteinase Complex from Aspergillus ochraceus L-1 with Fibrinolytic and Anticoagulant Activity

A complex of proteolytic enzymes with a specific plasmin-like activity of at least 890 EpNA/mg and a specific protein C activator activity of at least 130 EpNA/mg was isolated from the culture fluid of micromycete Aspergillus ochraceus L-1 by salting out with ammonium sulfate followed by dialysis and depigmentation to phenol-aniline formaldehyde resin at a pH of 8.2. Comparison of the obtained proteinase preparation with caseinolytic, fibrinolytic, fibrinogenolytic, and plasmin-like activities with commercial analogues terrilytin, trypsin, and streptokinase showed its promise for use as a means for thinning purulent burn wounds and fibrin clots. The resulting proteinase complex had high storage stability at low temperatures for up to 9 months.