PMID: 41165Sep 1, 1979

Proteolytic enzymes produced by Aspergillus ochraceus in relation to their plasma coagulating and fibrinolytic activities

V V KlechkovskaiaN S Egorov


The paper describes some properties of coagulases and fibrinolytic enzymes isolated from a proteolytic complex produced by Aspergillus ochraceus HP-19 during submerged cultivation on a synthetic medium. Proteolytic enzymes with the plasmocoagulating activity hydrolyzed casein at the maximum rate at 45 degrees C and pH 8.0--10.0. The coagulases were stable at pH 5.0--7.0 and were rather resistant to low pH values. The enzymes were entirely inactivated at 55 degrees C within 20--30 min. The activity of the coagulases was inhibited with the ions of Cu, Co, Ag, Pb, Mn, Zn and Hg (1.10(-3) M) by 100, 91, 85, 50, 50, 38 and 25%, respectively. The coagulases were entirely inhibited with EDTA whereas PCMB and PMSF inhibited their activity only to a small extent. The mechanism for blood clotting with the coagulases of Aspergillus ochraceus HP-19 is presumed to consist in the activation of protrombin via its limited specific proteolysis. The fibrinolytic enzymes of Aspergillus ochraceus HP-19 had the optimal pH 8.5 for casein, were stable at pH 6.0, and entirely inactivated at 55 degrees C within 5 min. In contrast to coagulases, they were resistant to the action of heavy metal ions. The enzymes were stabilized by the ions of Ca. The act...Continue Reading

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