ArticleBiotechnology letters2025
Optimization of recombinant neurturin expression in Escherichia coli using response surface methodology.
Article in Biotechnology letters, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
2 citing papers in PubMed.
- Comparison of Immunoprotective Efficacy of Six Antigenic Proteins ofPathogens (Basel, Switzerland) · 2026Article
- Rapid development of a robust cultivation process for subunit rotavirus vaccine antigen expression in Escherichia coli with the quality by design approach.Bioprocess and biosystems engineering · 2026Article
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Authors and funding
3 authors.
Funding
Abstract
Neurturin, a neurotrophic growth factor, has been identified as a potential treatment or reversal agent for neurodegenerative conditions. Although Escherichia coli is an appropriate host for recombinant protein expression, the production of proteins with disulfide bonds, such as neurturin, in this strain is frequently accompanied by the formation of inclusion bodies. In this study, the Rosetta-gami strain, which is well-suited for the accurate formation of disulfide bonds was employed for the soluble production of neurturin. Response surface methodology (RSM) was also used to investigate the effects of IPTG concentration, post-induction time and temperature on the soluble production of neurturin. The results showed that the highest yield of neurturin production occurred in the presence of 0.8 mM of IPTG after 5.5 h at 26 ºC. Fractional Factorial Design was used in the subsequent stage to screen the effects of culture medium components on the protein production. The best concentrations of yeast extract, tryptone and MgSO
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