Abstract
Abstract
The application of recombinant proteins is rare following the high production costs of expressing proteins with expensive inducers, such as isopropyl-β-D-1-thiogalactopyranoside (IPTG). Staphylokinase (SAK), a fibrinolytic enzyme, is a small bacterial thrombolytic agent that specifically clots and converts plasminogens to plasmins and lysis fibrin clots. The primary objective of the present investigation sought to increase the yield and lower the cost of staphylokinase production using Escherichia coli BL21 (DE3). Although the influence of the culture medium, culture density, and IPTG concentration on the production of SAK protein was explored. The results indicated that only culture density and concentration of IPTG were significant. This study achieved cost reduction by decreasing the IPTG inducer concentration (1.0 and 0.5 mM), which acted as the inducer. The production rate was also maintained or increased in low culture density. In conclusion, suitable production conditions, particularly diminished inducer concentration, effectively reduced upstream production costs and yielded high sak gene expression.
Publisher
Research Square Platform LLC
Reference23 articles.
1. High-level expression of non-glycosylated and active staphylokinase from pichia pastoris;Apte-Deshpnade A;Biotechnol Lett,2009
2. Recombinant protein folding and misfolding in Escherichia coli;Baneyx F;Nat Biotechnol,2004
3. Plasminogen Activators: a comparison;Baruah DB;Vascul Pharmacol,2006
4. Cloning and expression of hybrid streptokinase towards clot-specific activity;Buniya HK;J Microbiol methods,2014
5. Buniya HK, Farhan HA (2016) Cloning and Expression of Staphylokinase gene produced from Staphylococcus aureus in E. coli DH5α. Al-Anbar J Vet Sci 9: 7–14