Production, purification and Biochemical characterization of alkaline Fibrinolytic enzyme from Bacillus subtilisstrain-GBRC1

Jayalakshmi, Krishnamoorthy, Ramesh Babu, Vidhya
Journal of Chemical and Pharmaceutical Research   unpublished
Blood clots are formed from fibrinogen by thrombin and are lysed by plasmin, which is activated from tissue plasminogen activator. It was developed for the treatment of thrombosis because of its efficacy and strong affinity to fibrin. Due to the expense and undesirable side effects such as gastrointestinal bleeding, allergic reaction, and resistance to repercussion. Therefore the search for thrombolytic agents from other source is needed. Production of fibrinolytic enzyme from Bacillus subtilis
more » ... m Bacillus subtilis GBRC1is done by using nutrient broth medium. In addition, a strong fibrinolytic enzyme was purified from the cultivation media. The purified enzyme was almost homogeneous, as examined by SDS−PAGE and sephadex G-75 column chromatography. The enzyme had an optimal pH of 7-12 , an optimal temperature of 50 °C, for fibrin hydrolysis. The molecular mass estimated by gel filtration was 24.6 to 33.0kDa. Phenyl methyl sulphonyl fluoride almost completely inhibited the activity of the enzyme. Futher studies are necessary for the elucidation of their medicinal applications and molecular biological characteristics.
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