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Isolation, Screening and Characterization of ß-Haemolytic Streptococci with Potential of Streptokinase Production

Author Affiliations

  • 1Department of Microbiology, Karpagam University, Coimbatore, Tamil Nadu, INDIA
  • 2 Department of Microbial Biotechnology, Bharathiar University, Coimbatore, Tamil Nadu, INDIA
  • 3 Department of Microbiology, Centre for Advanced Studies in Biosciences, Jain University, Bangalore, INDIA

Int. Res. J. Biological Sci., Volume 2, Issue (4), Pages 63-66, April,10 (2013)

Abstract

Streptokinase is a novel fibrinolytic protein produced by several species of streptococci. As a therapeutic, streptokinase can be used in the treatment of thromboembolic disorderswhere it dissolves a blood clot by the activation of plasminogen to plasmin. Specimens from infected throat can be an excellent source for the isolation of haemolytic organisms. From the 34 throat swabs collected from patients with acute tonsillitis, 43 bacterial isolates demonstrated -haemolysis. Among thesehaemolytic organisms, 11 isolates were streptococci.Screening the isolates for their potency to producestreptokinase was an important criterion of this paper. Based on the results of radial caseinolysis assay and blood clot dissolving assay, isolate SK-6 demonstrated the highest streptokinase activity. When subjected to morphological and biochemical characterization based on Bergey’s criteria, isolate SK-6 was identified as Streptococcus equisimilis.The thrombolytic potential of this particular isolate indicated that it may also be utilized for the large scale production ofstreptokinase.

References

  1. Abdelghani T.T.A., Kunamneni A. and Ellaiah P., Isolation and mutagenesis of streptokinase producing bacteria,Am. J. Immunol., 1(4), 125-129 (2005)
  2. Hamid M., Rehman K.U. and Nejadmoqaddam M. R., Investigation of fibrinolytic activity of locally produced streptokinase,Asian J. Chem.23(1), 251-254 (2011)
  3. Banerjee A., Chisti Y. and Banerjee U.C., Streptokinase- a clinically useful thrombolytic agent, Biotechnol. Adv.,22(4), 287-307 (2004)
  4. Kumar A., Pulicherla K.K., Seetha Ram K. and Sambasiva Rao K.R.S., Evolutionary trend of thrombolytics, Int. J. BioSci. BioTechnol., 2(4), 51-68 (2010)
  5. Sha J., Galindo C.L., Pancholi V., Popov V.L., Zhao Y., Houstan C.W. and Chopra A.K., Differential expression of the enolase gene under in vivo versus in vitro growth conditions of Aeromonas hydrophila, Microb. Pathogenesis,34(4), 195-204 (2003)
  6. Dubey R., Kumar J., Agrawala D., Char T. and Pusp P., Isolation, production, purification, assay and characterization of fibrinolytic enzymes (Nattokinase, Streptokinase and Urokinase) from bacterial sources, Afr. J. Biotechnol.,10(8), 1408-1420 (2011)
  7. Mundada L.V., Prorok M., DeFord M.E., Figuera M., Castellino F.J. and Fay W.P., Structure–function analysis of the streptokinase amino terminus (residues 1–59), J. Biol. Chem., 278, 24421-24427 (2003)
  8. Mahboubi A., Sadjady S.K., Abadi M.M.S., AzadiS. and Solaimanian R., Biological activity analysis of native and recombinant streptokinase using clot lysis and chromogenic substrate assay, Iranian J. Pharma. Res., 11(4), 1087-1093 (2012)
  9. Malke H., Polymorphism of the streptokinase gene: implications for the pathogenesis of poststreptococcal glomerulonephritis, Zentralbl Bakteriol.,278(2-3), 246–257 (1993)
  10. Felsia X.F., Vijayakumar R. and Kalpana S., Production and partial purification of streptokinase from Streptococcus pyogenes, J.Biochem. Tech.,3(3), 289-291(2011)
  11. Babashmasi M., Razavian M.H. and Nejadmoghaddam M.R., Production and purification of streptokinase by protected affinity chromatography, Avicenna J. Med. Biotech.,1(1), 47-51 (2009)
  12. Saksela O., Radial caseinolysis in agarose: a simple method for detection of plasminogen activators in the presence of inhibitory substances and serum, Anal. Biochem., 111(2),276-282 (1981)
  13. Wu X.C., Ye R., Duan Y. and Wong S.L., Engineering of plasmin-resistant forms of streptokinase and their production in Bacillus subtilis: Streptokinase with longer functional half-life, Appl. Environ. Microbiol.,64(3), 824–829 (1998)
  14. Prasad S., Kashyap R.S., Deopujari J.Y., Purohit H.J., Taori G.M. and Daginawala H.F., Development of an in vitro model to study clot lysis activity of thrombolytic drugs,Thromb. J., 4, 14 (2006)
  15. Bergey D.H. and Holt J.G., Bergey’s manual of determinative bacteriology, 9th edn., Lippincott Williams and Wilkins, Philadelphia (2000)
  16. Hermentin P., Cuesta-Linker T., Weisse J., Schmidt K.H., Knorst M., Scheld M. and Thimme M. Comparative analysis of the activity and content of different streptokinase preparations, Eur. Heart J.,26, 933-940 (2005)
  17. World Health Organization, WHO Model List of Essential Medicines, 17th List, (2011) , Available at: http://whqlibdoc.who.int/hq/2011/a95053_eng.pdf
  18. Doss H.M., Manohar M., Singh N.A., Mohanasrinivasan.V and Devi C.S., Studies on isolation, screening and strain improvement of streptokinase producing - hemolytic streptococci, World J. Sci. Technol.,1(3), 7-11 (2011)
  19. Steele D.B. and Stowers M.D., Techniques for selection of industrially important microorganisms, Annu Rev Microbiol., 45, 89-106 (1991)
  20. Lancefield R.C., A serological differentiation of human and other groups of hemolytic Streptococci, J Exp Med, 57, 571– 595 (1933)
  21. Vandamme P., Pot B., Falsen E., Kersters K. and Devriese L.A., Taxonomic study of Lancefield streptococcal groups C, G, and L (Streptococcus dysgalactiae) and proposal of S. dysgalactiae subsp. equisimilis subsp nov, Int. J. Syst. Bacteriol., 46, 774–81 (1996)
  22. Feldman L.J. Streptokinase manufacture, In German, German patent DE 2354019 (1974)
  23. Brandt C.M. and Spellerberg B.,Human infections due to Streptococcus dysgalactiae Subspecies equisimilis, Emerging Infections., 49(1), 767- 772 (2009)
  24. Christensen L.R., Streptococcal fibrinolysis: a proteolytic reaction due to serum enzyme activated by streptococcal fibrinolysin, J. Gen. Physiol.,28, 363– 383 (1945)