Purification of periplasmic bound recombinant shiga toxin B protein from Escherichia coli BL21 using two different rupture schemes: Osmotic shock and cell lysis.

摘要

The purpose of this research has been to investigate the purification of periplasmic bound recombinant shiga toxin B protein from E. coli BL21 using two different cell product release mechanisms: osmotic shock and cell lysis to determine which method is most efficient. The osmotic shock procedure involves the release of proteins located only in the periplasmic space of the cell thus resulting in a significantly more simplified product as compared to the whole cell lyse procedure that involves a complete cell rupture releasing all cellular proteins. The osmotic shock method initially was adapted but with its inability to be efficiently scaled up the understanding of a cell lysis scheme became of interest because of its ease in a large scale process. The potential benefits and use of shiga toxin B protein within vaccines, recently discovered, may result in an increase in demand and production thereby justifying this study.