Purification and Characterization of Fibrinolytic Enzyme by Bacillus cereus sdk1 from Vellar estuary, South East Coast of India

R Sadeesh kumar D Annadurai R Rajesh


Blood clots are formed from fibrinogen by thrombin and are lysed by plasmin, which gets activated from tissue plasminogen activator. Plasmin - derived bioactive compounds was developed for the treatment of thrombosis because of its efficacy and strong affinity to fibrin. Prevailing drugs are highly expensive and leads to 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 cereus SDK1 was done using Nutrient broth medium. In addition, a strong fibrinolytic enzyme was purified from the cultivation media. The purified enzyme was almost homogeneous with other species of same genus, 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 to36 KDa. Phenyl methyl sulphonyl fluoride almost completely inhibited the activity of the enzyme. Further studies for characterization and structural elucidation are necessary for their medicinal applications and molecular biological characteristics.

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