ArticleAMB Express2020
A novel and more efficient biosynthesis approach for human insulin production in Escherichia coli (E. coli).
Article in AMB Express, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 26 citations in OpenAlex.
- Genetically Modified Microorganisms: Risks and Regulatory Considerations for Human and Environmental Health.Microorganisms · 2026Review
- The response surface method enables efficient optimization of induction parameters for the production of bioactive peptides in fed-batch bioreactors using Escherichia coli.Folia microbiologica · 2026Article
- Optimizing proinsulin production in E. coli BL21 (DE3) using taguchi method and efficient one-step insulin purification by on-column enzymatic cleavage.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2025Article
- An Overview of Diverse Strategies To InactivateEcoSal Plus · 2023Review
- An elevated OmpA expression during the production of a recombinant protein in Escherichia coli.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2023Article
- Synthetic biology-inspired cell engineering in diagnosis, treatment, and drug development.Signal transduction and targeted therapy · 2023Review
- Guided extraction of genome-scale metabolic models for the integration and analysis of omics data.Computational and structural biotechnology journal · 2021Article
- Cloning, expression and purification of recombinant dermatopontin in Escherichia coli.PloS one · 2020Article
Corrections and comments
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
Abstract
Insulin has captured researchers' attention worldwide. There is a rapid global rise in the number of diabetic patients, which increases the demand for insulin. Current methods of insulin production are expensive and time-consuming. A PCR-based strategy was employed for the cloning and verification of human insulin. The human insulin protein was then overexpressed in E. coli on a laboratory scale. Thereafter, optimisation of human insulin expression was conducted. The yield of human insulin produced was approximately 520.92 (mg/L), located in the intracellular fraction. Human insulin was detected using the MALDI-TOF-MS and LC-MS methods. The crude biosynthesised protein sequence was verified using protein sequencing, which had a 100% similarity to the human insulin sequence. The biological activity of human insulin was tested in vitro using a MTT assay, which revealed that the crude biosynthesised human insulin displayed a similar degree of efficacy to the standard human insulin. This study eliminated the use of affinity tags since an untagged pET21b expression vector was employed. Tedious protein renaturation, inclusion body recovery steps, and the expensive enzymatic cleavage of the C-peptide of insulin were eliminated, thereby making this method of biosynthesising human insulin a novel and more efficient method.
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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.