Production, purification, and biochemical characterization of a fibrinolytic enzyme from thermophilic Streptomyces sp. MCMB-379.

Production of the fibrinolytic enzyme was carried out using 2.5-L glass fermentor, culture of thermophilic Streptomyces sp., and glucose yeast extract peptone medium of pH 8.0. Five successive batches were carried out under controlled fermentation conditions viz., agitation 140 rpm, aeration 0.5 vvm, 55 °C, and 18 h. The total protein extracellularly produced in the cell-free broth was ~300-500 mg/L. The enzyme belongs to serine endopeptidase type. Studies on the fibrin degradation indicate that the enzyme degrades the fibrin into small molecular weight products as seen from HPLC profile. Phase-contrast microscopic structure of fibrin showed that enzyme cleaves the fibrin filaments. The ex vivo activity of the actinokinase was compared with 500 IU of urokinase and 350 IU of streptokinase. The ex vivo clot lysis was found to be faster as compared to the commercial available enzymes.