Purification and characterization of fibrinolytic metalloprotease from Perenniporia fraxinea mycelia

Characterization and Production of Thermostable and Acid-stable Extracellular Fibrinolytic Enzymes from Cordyceps militaris

“…The enzyme was highly stable in a pH range of 4-9 at 37 o C for 1 h, and more than 80% of its activity sustained. These results were quite similar to those of the proteolytic enzyme from C. militaris (Choi et al, 2010;Maki et al, 2005), C. sinensis , nematode-trapping fungi (Wang et al, 2006), and P. fraxinea (Kim et al, 2008). Proteases of entomopathogenic fungus P. farinosus showed an optimum pH of 8.5 using fluorescein isothiocyanate-casein as the substrate.…”

“…Extracellular protease with fibrinolytic activity from the culture supernatant of Cordyceps sinensis was 31 kDa . The molecular weights were determined for the proteaes from A. oligospora (35.2 kDa) (Tunlid et al, 1994), A. frondosa (20 kDa), A. mellea (32 kDa), D. varietas (30 kDa) , Perenniporia fraxina mycelia (42 kDa) (Kim et al, 2008) and Fusarium sp CPCC480097 (28 kDa) (Wu et al, 2009). As a result, it is obvious that entomopathogenic fungi and nematophagous fungi produce various proteolytic enzymes to degrade insect cuticle.…”

Fibrinolytic Enzymes from Medicinal Mushrooms

“…Previous studies have demonstrated that the fibrinolytic enzymes may be available in the fruiting bodies of some mushrooms but not in the cultured mycelium (Kim et al, 2008). The purification stratagem for these extracellular fibrinolytic enzymes differs from those of fruiting bodies or mycelium.…”

“…Choi and Sa (2000) isolated a metalloprotease with fibrinolytic activity from cultured mycelium of Ganoderma lucidum (Choi & Sa, 2000). In the following decade, fibrin(ogen)olytic proteases from mushroom mycelium, including metalloprotease from A. mellea (AMMP), metalloprotease from F. velutipes FVP-1, and metalloprotease from Perenniporia fraxinea, were identified (Kim et al, 2008;Lee et al, 2005;Park et al, 2007). Fibrinolytic metalloproteases are sensitive to metalloprotease inhibitors (e.g., EDTA and 1,10-phenanthroline) and metal ions.…”

Fibrin(ogen)olytic and antiplatelet activities of a subtilisin-like protease from Solanum tuberosum (StSBTc-3)

“…Preferences in the digestion of fibrinogen chains of AMP48; Codiase and StSBTc-3 make a difference between these plant proteases and proteases with fibrinogenolytic activity from other sources. a-fibrinogenase from different sources including snake venom [32], Lampetra japonica [33], Codium species [34,35], Paecilomyces tenuipes [36], and Perenniporia fraxinea [37] preferentially hydrolyze a-subunit. However, the g-chain does not appear to be a second specific target.…”