Potent fibrinolytic enzyme from a thermophilic Streptomyces megasporus strain SD5.
As a therapeutic agent in thrombosis the fibrinolytic enzymes are of interest and the search for a new enzyme continues. A strong fibrin-specific fibrinolytic enzyme was purified from the cell-free spent broth of thermophilic Streptomyces megasporus strain SD5. The crude enzyme was concentrated using ammonium sulphate, dialysis and lyophilization. Approximately 0.11 mg ml(-1) crude enzyme with a specific activity of 4.2 U microg(-1) was obtained. Post-electrophoretic reactivity revealed a monomeric form of the enzyme with a molecular weight of 35 kDa. The optimum pH and temperature for production of the enzyme were 8 and 55 degrees C, respectively. The enzyme was resistant to a broad range of pH ranging from 6 to 9 and temperature ranging from 37 to 60 degrees C. The enzyme was a chymotrypsin-like serine peptidase and the activity of the enzyme was N-terminal-dependent. The in vitro clot lysis by the enzyme at 37 degrees C was encouraging.
Chitte
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Division of Microbial Sciences, M.A.C.S. Agharkar Research Institute, Pune, Maharashtra, India.
Dey
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D005342:Fibrinolysis; D005343:Fibrinolytic Agents / Q000302:isolation & purification*; D006358:Hot Temperature; D012697:Serine Endopeptidases / Q000302:isolation & purification*; D013302:Streptomyces / Q000201:enzymology*; D013379:Substrate Specificity; D014871:Water Microbiology
D005343:Fibrinolytic Agents; D012697:Serine Endopeptidases