Optimization of fibrinase productivity from Actinomycetes

Background: Fibrinolytic enzymes that dissolve blood clots and show promise for thrombosis therapy have been successfully identified from various sources. A wide range of microorganisms has been screened for their fibrinolytic properties. A fibrinolytic protease has been isolated from Streptomyces violaceoruber and Streptomyces spiroverticillatus culture filtrate. Methods : The purification procedure involved ammonium sulphate fractionation, dialysis, calcium phosphate gel purification and gel filtration on Sephadex G-100. By using native polyacrylamide gel electrophoresis (Native PAGE) to determine molecular weight of the enzyme. Results : The optimum temperature for the high production of fibrinase from S. violaceoruber was 30oC and from S. spiroverticillatus was 35oC and the optimum pH was 9.0. The best incubation period is 6 days. The incorporation of lactose as carbon source, yeast extract as nitrogen source and MnCl2 to culture media highly increased the production of fibrinase from the two species. The molecular weight was about 30 KDa. Conclusion: It exhibited fibrinolytic enzyme activity. In vitro studies revealed that fibrinase dissolves clots made by blood.