ArticleJournal of pharmacy & bioallied sciences2019
Optimization of Secreted Recombinant Human Epidermal Growth Factor Production Using Pectate Lyase B from
Article in Journal of pharmacy & bioallied sciences, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 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
6 citing papers in PubMed, 16 citations in OpenAlex.
- Essential factors, advanced strategies, challenges, and approaches involved for efficient expression of recombinant proteins in Escherichia coli.Archives of microbiology · 2024Review
- EGF, a veteran of wound healing: highlights on its mode of action, clinical applications with focus on wound treatment, and recent drug delivery strategies.Archives of pharmacal research · 2023Review
- Article
- Continuous Production of Human Epidermal Growth Factor UsingFrontiers in microbiology · 2022Article
- Activity and Effectiveness of Recombinant hEGF Excreted byJournal of experimental pharmacology · 2020Article
- Stabilization of eye drops containing autologous serum and recombinant human epidermal growth factor for dry eye syndrome.Journal of advanced pharmaceutical technology & researchArticle
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
contextHuman Epidermal Growth Factor (hEGF) is a potential therapeutic protein that has been widely used as a healing agent for various chronic wounds. It induces the proliferation and metabolism of epithelial cells, regenerates skin cells, and validates skin elasticity. In the previous study, recombinant hEGF (rhEGF) had been successfully expressed extracellularly in Escherichia coli (E. coli) BL21 (DE3) using pectate lyase B (PelB) signal peptide. The previous study has shown that the medium concentration and the induction time influenced the production of rhEGF.
aimsTherefore, this study was conducted to optimize the induction time and medium concentration for rhEGF extracellular secretion then followed by scale-up production. SETTINGS AND
designThis experiment was carried out using E. coli BL21 (DE3) which contains pD881 plasmid that carries hEGF and PelB gene. Optimization design of induction time and medium concentration were obtained using Central Composite Design (CCD). METHODS AND MATERIAL: The method of study started by the rejuvenation of E. coli culture, extracellular secretion, and optimization in the flask scale then followed by scaled-up production with high-cell density culture in the fermenter. STATISTICAL ANALYSIS USED: The optimization was carried out using Response Surface Methodology (RSM) and multi regression analysis.
resultsThis work showed that the multiplication of 1.5-fold medium concentration with induction time 3h after the culture started gave the best result among another condition in this study. Additionally, the rhEGF production in the fermenter scale was identified by SDS-PAGE Tricine and quantified by ELISA, which showed 122.40 μg of the rhEGF per milliliter medium.
conclusionsIn respect of the result, we conclude that the optimized condition of extracellular secretion was successfully obtained, and gives higher result before the previous study.
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