ArticleIranian journal of pharmaceutical research : IJPR2015
Enhanced Production of Insulin-like Growth Factor I Protein in Escherichia coli by Optimization of Five Key Factors.
Article in Iranian journal of pharmaceutical research : IJPR, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 18 citations in OpenAlex.
- Efficient in vivo removal of solubility tag to improve the bacterial production of soluble, bioactive human IGF-1.World journal of microbiology & biotechnology · 2026Article
- Proteomic Analysis of Plant-Derived hIGF-1-Fc Reveals Proteome Abundance Changes Associated with Wound Healing and Cell Proliferation.Proteomes · 2025Article
- Comparing the Soluble Form of Recombinant Human Insulin-like Growth Factor-1 (rhIGF-1) inProtein and peptide letters · 2024Article
- Acetate Kinase a Antisense Delivery by PAMAM Dendrimer for Decreasing Acetate Production and Increasing the Production of Recombinant Albumin inIranian journal of biotechnology · 2021Article
- Review Insights In Cardiac Tissue Engineering: Cells, Scaffolds, and Pharmacological Agents.Iranian journal of pharmaceutical research : IJPR · 2021Review
- Optimization and One-Step Purification of Recombinant V Antigen Production from Yersinia pestis.Molecular biotechnology · 2020Article
- Optimization of Key Factors in Serum Free Medium for Production of Human Recombinant GM-CSF Using Response Surface Methodology.Iranian journal of pharmaceutical research : IJPR · 2019Article
- Optimization of Growth Conditions ofIranian journal of pharmaceutical research : IJPR · 2018Article
- Expression and Secretion of Endostar Protein by Escherichia Coli: Optimization of Culture Conditions Using the Response Surface Methodology.Molecular biotechnology · 2016Article
- Effect of Culture Condition Variables on Human Endostatin Gene Expression inJundishapur journal of microbiology · 2016Article
- The effect of cell disruption techniques and chaotropic agents on the downstream purification process of mecasermin produced as inclusion body in E. coli.Research in pharmaceutical sciencesArticle
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Human insulin-like growth factor I (hIGF-I) is a kind of growth factor with clinical significance in medicine. Up to now, E. coli expression system has been widely used as a host to produce rhIGF-1 with high yields. Batch cultures as non-continuous fermentations were carried out to overproduce rhIGF-I in E. coli. The major objective of this study is over- production of recombinant human insulin-like growth factor I (rhIGF-I) through a developed process by recruiting effective factors in order to achieve the most recombinant protein. In this study we investigated the effect of culture medium, induction temperature and amount of inducer on cell growth and IGF-1 production. Taguchi design of experiments (DOE) method was used as the statistical method. Analysis of experimental data showed that maximum production of rhIGF-I was occurred in 32y culture medium at 32 °C and 0.05 Mm IPTG. Under this condition, 0.694 g/L of rhIGF-I was produced as the inclusion bodies. Following optimization of these three factors, we have also optimized the amount of glucose and induction time in 5 liter top bench bioreactor. Full factorial design of experiment method was used for these two factors as the statistical method. 10 g/L and OD600=5 were selected as the optimum point of Glucose amount and induction time, respectively. Finally, we reached to a concentration of 1.26 g/L rhIGF-1 at optimum condition.
Indexed as
Identifiers
26330880PMC4518120W1921990899What 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.