ArticleMaedica2012
Optimizing of Nutrients for High Level Expression of Recombinant Streptokinase Using pET32a Expression System.
Article in Maedica, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 14 citations in OpenAlex.
- Cloning, expression and purification of antigenic fragments of theIranian journal of microbiology · 2022Article
- Engineering synthetic microbial consortium for cadaverine biosynthesis from glycerol.Biotechnology letters · 2022Article
- Expression of Bacillus amyloliquefaciens transglutaminase in recombinant E. coli under the control of a bicistronic plasmid system in DO-stat fed-batch bioreactor cultivations.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2021Article
- Engineering a pyridoxal 5'-phosphate supply for cadaverine production by using Escherichia coli whole-cell biocatalysis.Scientific reports · 2015Article
- Functional expression of recombinant human trefoil factor 1 by Escherichia coli and Brevibacillus choshinensis.BMC biotechnology · 2015Article
- Article
- Isolation, cloning, and expression of E. coli BirA gene for biotinylation applications.Advanced biomedical research · 2015Article
- Overexpression and Enzymatic Assessment of Antigenic Fragments of Hyaluronidase Recombinant Protein From Streptococcus pyogenes.Jundishapur journal of microbiology · 2015Article
- Cloning and expression of the enzymatic region of Streptococcal hyaluronidase.Iranian journal of basic medical sciences · 2014Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Streptokinase (SK) is being increasingly used in the treatment of acute myocardial infarction and ischemic stroke. The feeding control method using substrate balance equations is vital to maintain the preferred specific growth rate for the high-level expression of recombinant proteins. In this study, initial experiments on chemical and temperature inducible expression systems were carried out to identify appropriate expression conditions to improve production of recombinant Streptokinase. Streptokinase gene of group C Streptococci was cloned into prokaryotic expression vector pET32a. Gene expression was optimized by changing levels of glucose, tryptone, and MgSO4 in the media and temperature-inducible expression system and recombinant protein was confirmed by western blot analysis with anti streptokinase sera of immunized rats. Among the various expression systems used, the quantity of recombinant streptokinase produced in the medium containing 2.4% glucose was more than two-fold compared to the medium containing 0.2% glucose. In addition, temperature induction system (37°C) was found to result in higher productivities compared to room temperature. In conclusion we have demonstrated that significant improvement in the streptokinase yield can be obtained by modifying the media and feeding of substrate. These results indicate that efficient process control strategy is important for the mass production of streptokinase.
Indexed as
Identifiers
23400422PMC3566888W2143604699What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.