ArticleBioengineered2017
High purity recombinant human growth hormone (rhGH) expression in Escherichia coli under phoA promoter.
Article in Bioengineered, 2017. 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, 25 citations in OpenAlex.
- Delaying production with prokaryotic inducible expression systems.Microbial cell factories · 2024Review
- RNA-seq reveals multifaceted gene expression response to Fab production in Escherichia coli fed-batch processes with particular focus on ribosome stalling.Microbial cell factories · 2024Article
- In silico and in vitro analysis of a rational mutation in gIII signal peptide and its effects on periplasmic expression of rhGH in E. coli.Archives of microbiology · 2022Article
- Fusion Tag Design Influences Soluble Recombinant Protein Production inInternational journal of molecular sciences · 2022Article
- Upstream development of Escherichia coli fermentation process with PhoA promoter using design of experiments (DoE).Journal of industrial microbiology & biotechnology · 2020Article
- Scalable, two-stage, autoinduction of recombinant protein expression in E. coli utilizing phosphate depletion.Biotechnology and bioengineering · 2020Article
- Escherichia coli "TatExpress" strains export several g/L human growth hormone to the periplasm by the Tat pathway.Biotechnology and bioengineering · 2019Article
- Systematic Evaluation of Genetic and Environmental Factors Affecting Performance of Translational Riboswitches.ACS synthetic biology · 2019Article
- Efficient production of human zona pellucida-3 in a prokaryotic expression system.World journal of microbiology & biotechnology · 2018Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
ABSTACT Recombinant human Growth Hormone (rhGH) is an important protein for human growth and is in high demand in clinics. Hence, it is necessary to develop an efficient fermentation process to produce highly pure rhGH. In this study, rhGH was expressed in Escherichia coli under alkaline phosphatase (phoA) promoter. The cultivation conditions for high expression level and purity of rhGH were investigated. The best initial phosphate concentration for rhGH expression, out of the 4 levels of initial phosphate concentration tests performed, was 12.6 mmol/L. Subsequently, 2 fed-batch cultivations under low dissolved oxygen (DO) (0% - 10%) and high DO (20% - 30%) conditions were carried out. High purity rhGH (92%) was obtained from 20% - 30% DO-stat cultivation, although the biomass did not show any significant difference. In summary, this research provided an efficient fermentation process for high purity rhGH production from E. coli under phoA promoter, which can lower the production and purification costs for large-scale production of rhGH.
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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.