PRODUCTION AND PARTIAL CHARACTERIZATION OF FIBRINOLYTIC ENZYME FROM A SOIL ISOLATE ASPERGILLUS CARBONARIUS S-CSR-0007

Afini A.v. M., Sooraj S. Nath, Smitha K. V., Kunhi A.a. M.
2016 International Journal of Pharmacy and Pharmaceutical Sciences  
<p><strong>Objective: </strong>This work was undertaken with the aim of isolating and screening fungal soil isolates with fibrinolytic activity.</p><p><strong>Methods: </strong>Soil sample near slaughter house was collected and screened for fibrinolytic activity by using fibrin-agar. Enzyme production was optimized under various parameters like pH, temperature, substrate concentration and purified partially by ammonium sulphate precipitation. The stability of the partially purified enzyme was
more » ... rified enzyme was analyzed under the influence of a wide range of pH, temperature, and substrate concentrations.<strong></strong></p><p><strong>Results: </strong>Among the seven isolates screened, Aspergillus carbonarius S-CSR-0007 exhibited largest clear zone and was selected for further studies. Among the various substrates tested casein was found to support the highest caseinolytic activity of 816 U/ml and fibrinolytic activity of 510 U/ml. The culture supernatant of A. carbonarius S-CSR-0007 was fractionated by ammonium sulfate precipitation followed by dialysis, and maximum activity was obtained in the fraction with 80% ammonium sulfate, with an enzyme activity of 1200 U/ml using tyrosine as standard. The partially purified fibrinolytic enzyme showed optimal activity at 45 °C and pH 7.0. The enzyme was stable up to a temperature of 50 °C and pH 8.0, and the optimum substrate concentration was 4%.</p><p><strong>Conclusion: </strong>The crude enzyme showed high blood clot lysis activity, which may be a good candidate in the pharmaceutical industry. However, more studies need to be carried out to establish its clinical use.</p>
doi:10.22159/ijpps.2016v8i12.15069 fatcat:2wwjrc2lnfdwvhiy2i35qe7vqi