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

• Published in: Moscow University biological sciences bulletin Vol. 75; no. 3; pp. 130 - 135
• Main Authors: Osmolovskiy, A. A., Orekhova, A. V., Conti, E., Kreyer, V. G., Baranova, N. A., Egorov, N. S.
• Format: Journal Article
• Language: English
• Published: Moscow Pleiades Publishing 01.07.2020; Springer Nature B.V
• Subjects: Ammonium; Ammonium sulfate; Aniline; Anticoagulants; Aspergillus ochraceus; Biochemistry; Biomedical and Life Sciences; Cell Biology; Dialysis; Fibrin; Life Sciences; Low temperature; Plant Sciences; Plasmin; Protein C; Proteinase; Proteolysis; Proteolytic enzymes; Research Article; Shelf life; Streptokinase; Trypsin; Zoology; hemostatic-active compounds; enzyme stability; micromycete proteinases; enzyme preparations; fibrinolytic activity; depigmentation
• ISSN: 0096-3925; 1934-791X
• DOI: 10.3103/S0096392520030074

— A complex of proteolytic enzymes with a specific plasmin-like activity of at least 890 E pNA /mg and a specific protein C activator activity of at least 130 E pNA /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.