ArticleJournal, genetic engineering & biotechnology2023
Codon optimization of a gene encoding DNA polymerase from Pyrococcus furiosus and its expression in Escherichia coli.
Article in Journal, genetic engineering & biotechnology, 2023. 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.
- Recombinant Thermostable DNA Polymerases: Current Approaches to Production, Molecular Engineering, and Applications in Biotechnology and Diagnostics.International journal of molecular sciences · 2026Review
- Immunoinformatics-guided design of a multi-epitope vaccine targeting WISP1 for gastric cancer.BMC biotechnology · 2026Article
- Immunoinformatic design of a multi-epitope vaccine candidate targeting multidrug-resistant Pseudomonas aeruginosa.BMC immunology · 2026Article
- Immunoinformatic-driven design of a multi-epitope vaccine againstBiochemistry and biophysics reports · 2026Article
- CodonTransformer: a multispecies codon optimizer using context-aware neural networks.Nature communications · 2025Article
- Bioinformatics analysis of the in silico engineered protein vaccine with and without Escherichia coli heat labile enterotoxin adjuvant on the model of Klebsiella pneumoniae.Scientific reports · 2025Article
- An efficient approach for overproduction of DNA polymerase from Pyrococcus furiosus using an optimized autoinduction system in Escherichia coli.World journal of microbiology & biotechnology · 2024Article
- Design of multi-epitope vaccine candidate based on OmpA, CarO and ZnuD proteins against multi-drug resistantHeliyon · 2024Article
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Authors and funding
6 authors.
Funding
Abstract
backgroundDNA polymerase is an essential component in PCR assay for DNA synthesis. Improving DNA polymerase with characteristics indispensable for a powerful assay is crucial because it can be used in wide-range applications. Derived from Pyrococcus furiosus, Pfu DNA polymerase (Pfu pol) is one of the excellent polymerases due to its high fidelity. Therefore, we aimed to develop Pfu pol from a synthetic gene with codon optimization to increase its protein yield in Escherichia coli.
resultsRecombinant Pfu pol was successfully expressed and purified with a two-step purification process using nickel affinity chromatography, followed by anion exchange chromatography. Subsequently, the purified Pfu pol was confirmed by Western blot analysis, resulting in a molecular weight of approximately 90 kDa. In the final purification process, we successfully obtained a large amount of purified enzyme (26.8 mg/L). Furthermore, the purified Pfu pol showed its functionality and efficiency when tested for DNA amplification using the standard PCR.
conclusionsOverall, a high-level expression of recombinant Pfu pol was achieved by employing our approach in the present study. In the future, our findings will be useful for studies on synthesizing recombinant DNA polymerase in E. coli expression system.
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