Purification of recombinant streptokinases by Ion-exchange chromatography
Journal Title: International Research Journal of Applied and Basic Sciences - Year 2015, Vol 9, Issue 5
Abstract
Streptokinase is novel fibrinolytic enzymes which are isolated from Bacillus subtilis, ?-haemolytic Streptococci sample. The purpose of the study was to Recombinant protein purification and subject that to separation improvement using ion exchange chromatography for enhanced streptokinase production. The solubility and yield of pure protein are highly dependent on various combinations of chemical additives, ionic and non-ionic detergents and buffer, with solubilizing agents followed by refolding of denatured protein into active form. It was seen using high expression systems gave enhance streptokinase activity in comparison to the another system. Rate exclusion ion exchange chromatography profile shows that there are minimal aggregates in the active streptokinase protein and the percentage of renaturation is estimated 98%.The maximum specific activity of the purified streptokinase was achieved by these methods. The refolded recombinant streptokinase was analyzed by RP-HPLC showing a purity of 98%.
Authors and Affiliations
H. azadi*| M. Sc .Research Student of Chemical Engineering ,Science and Research Branch ,Islamic Azad university ,Tehran ,Iran, email: hani_azadi@yahoo.com, A. Heidarinasab| Associate Professor of Chemical Engineering ,Science and Research Branch ,Islamic Azad university ,Tehran ,Iran, A. Seifkordi| Associate Professor of Chemical Engineering ,Science and Research Branch ,Islamic Azad university ,Tehran ,Iran
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