Purification and characterization of a novel fibrinolytic protease from Schizophyllum commune
Schizophyllum commune, a widely distributed medicinal mushroom, was found with fibrinolytic activity from its basidiomycetes. The fibrinolytic activity of S. commune was to be beneficial for antithrombotic therapy. In this study, S. commune was cultured with fermentation technology, and protease purification was carried out by cross-flow filtration and fast performance liquid chromatography (FPLC) system. The specific activity of S. commune fibrinolytic protease increased 9.29-fold over the culture broth after purification. The fibrinolytic protease shows superior fibrinolytic activity than human plasmin and is inhibited by EDTA. Characterizations of this protease showed 21.32 kDa in molecular mass and monomeric form in protein structure. The optimal protease activity reveals at pH 5.0 and 45°C, and is enhanced by magnesium.
Lu, C.-L.; Chen, S.; and Chen, S.-N.
"Purification and characterization of a novel fibrinolytic protease from Schizophyllum commune,"
Journal of Food and Drug Analysis: Vol. 18
, Article 4.
Available at: https://doi.org/10.38212/2224-6614.2283