Partial Purification and Biochemical Evaluation of Protease Fraction (MA-1) from Mycoleptodonoides aitchisonii and Its Fibrinolytic Effect

The antioxidative proteolytic fraction, MA-1, was partially purified from Mycoleptodonoides aitchisonii. MA-1 to homogeneity using a two-step procedure, which resulted in an 89-fold increase specific activity and 42.5% recovery. SDS-PAGE revealed two proteins with molecular weight of 48 kDa. zymography results based on the band. found be stable presence Na+, Ca2+, Fe3+, K+, Mg2+. also methanol, ethanol, acetone, its enzyme increased by 15% SDS. inhibited ethylenediaminetetra-acetic acid or ethylene glycol tetraacetic exerted highest specificity for substrate, MeO-Suc-Arg-Pro-Tyr-pNA, chymotrypsin. Accordingly, belongs family chymotrypsin-like metalloproteins. optimum temperature 40 °C stability range 20 35 °C. pH were 5.5 4–11. exhibited stronger fibrinolytic than plasmin. hydrolyzed Aα, Bβ, γ chains fibrinogen within 2 h. antithrombotic effect animal models. devoid hemorrhagic at dose 80,000 U/kg. Overall, our show that M. aitchisonii produces acid-tolerant enzyme, containing could beneficial functional material prevention cardiovascular diseases possible complications.