ISOLATION, PRODUCTION, ASSAY AND CHARACTERIZATION OF FIBRINOLYTIC ENZYMES (NATTOKINASE AND STREPTOKINASE) FROM BACTERIA
DOI:
https://doi.org/10.48047/Keywords:
Anticoagulant activity, Protein fraction precipitation, casein, serum and plasminogen plate technique, enzyme thermodynamics, expression system, zymography, Edman degradationAbstract
Nattokinase, and Streptokinase are novel fibrinolytic enzymes which are isolated from Bacillus subtilis, β-haemolyti
Streptococci and urine sample. The fibrinolytic enzyme Nattokinase, and Streptokinase was purified from
supernatant of Bacillus subtilis, β-haemolytic Streptococci and recombinant E.coli containing short fragment
genomic DNA of Pseudomonas sp. Culture broth and showed thermophilic, hydrophilic, and strong fibrinolytic
activity. The optimum temperature and pH of Nattokinase, Streptokinase were 37-55°C and 9, 27-37°C and 9,
respectively. The molecular weight of Nattokinase, Streptokinase was approximately 28 kDa, 47 kDa and 34 kDa,
respectively, as determined by sodium dodecyl sulfatepolyacrylamide gel electrophoresis. The caseinolytic activity
of Nattokinase, and Streptokinase 576.73 U, 467.73 U respectively, while fibrinolytic activity achieved by fibrin
plate method were 10 U, 5 U respectively.
