Abstract

PURIFICATION AND BIOCHEMICAL CHARACTERIZATION OF A NOVEL FIBRINOLYTIC PROTEASE FROM STAPHYLOCOCCUS AUREUS MTCC 902

K. S. Dayananda*, Shweta Joshi, S.M. Gopinath, Ismail Shareef and Jagan Mohan Reddy. P, Ajay Mandal

Abstract

Fibrinolytic enzymes are protease enzyme that helps in treating cardiovascular diseases. Microorganisms are easily available and less expensive source of fibrinolytic enzyme. Fibrinolytic protease (FP31) was purified from Staphylococcus aureus (MTCC 902) by sequential steps of precipitation by ammonium sulphate, Sephadex G- 75 and DEAE –Sephadex A- 50. After the purification of enzyme the activity was enhanced to 40.32 fold and 9.47% recovery was achieved. The optimum temperature was 40 ºC and the optimum pH was found to be 8. Activity was significantly blocked by EDTA, pefabloc and EGTA. All this indicates purified enzyme as a serinemetallo protease with application in thrombolytic therapy.

Keywords: Fibrinolytic enzyme, Cardiovascular diseases, Sephadex G-75, thrombolytic therapy, DEAE-Sephadex A-50.