High level intracellular expression of recombinant streptokinase as an inclusion body in E. coli

4^th International Conference and Exhibition on Biologics & Biosimilars

October 26-28, 2015 Baltimore, USA

Suthakaran Pichaimuthu1, Bilgimol C Joseph1 and Krishnakanth Pulicherla2

1Micro Therapeutic Research Labs Pvt. Ltd., India 2VIT University, India

Posters-Accepted Abstracts: J Bioanal Biomed

Abstract :

Streptokinase, a 414 amino acid polypeptide with molecular weight of 47 kDa, is a potent activator of the fibrinolytic system in humans. High level expression of recombinant protein in E. coli frequently results in accumulation of protein as insoluble aggregates known as inclusion bodies and they do offer several advantages. Expression as inclusion bodies is useful to obtain large amount of the protein, provided refolding is not difficult and recovery of the active protein is high. This is particularly true with the proteins not having disulfide bonds. Since streptokinase does not have disulfide bonds, the focus is to obtain higher quantity of stable protein as inclusion bodies. In the present study, an attempt was made to investigate the effect of temperature and post induction time on stable (non-degradable) expression of recombinant streptokinase of higher content as inclusion body in Escherichia coli.

Biography :

Email: suthabio1@gmail.com