ArticleJournal of industrial microbiology & biotechnology2012
Enhanced production of α-cyclodextrin glycosyltransferase in Escherichia coli by systematic codon usage optimization.
Article in Journal of industrial microbiology & biotechnology, 2012. 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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6 citing papers in PubMed, 24 citations in OpenAlex.
- Combined Optimization of Codon Usage and Glycine Supplementation Enhances the Extracellular Production of a β-Cyclodextrin Glycosyltransferase fromInternational journal of molecular sciences · 2020Article
- Heterologous expression of cyclodextrin glycosyltransferase from Paenibacillus macerans in Escherichia coli and its application in 2-O-α-D-glucopyranosyl-L-ascorbic acid production.BMC biotechnology · 2018Article
- High production of genistein diglucoside derivative using cyclodextrin glycosyltransferase from Paenibacillus macerans.Journal of industrial microbiology & biotechnology · 2017Article
- Efficient extracellular recombinant production and purification of a Bacillus cyclodextrin glucanotransferase in Escherichia coli.Microbial cell factories · 2017Article
- Expression of Codon-Optimized Plant Glycosyltransferase UGT72B14 in Escherichia coli Enhances Salidroside Production.BioMed research international · 2016Article
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5 authors at 2 institutions in 1 country.
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Abstract
Enhancing the production of α-cyclodextrin glycosyltransferase (α-CGTase) is a key aim in α-CGTase industries. Here, the mature α-cgt gene from Paenibacillus macerans JFB05-01 was redesigned with systematic codon optimization to preferentially match codon frequencies of Escherichia coli without altering the amino acid sequence. Following synthesis, codon-optimized α-cgt (coα-cgt) and wild-type α-cgt (wtα-cgt) genes were cloned into pET-20b(+) and expressed in E. coli BL21(DE3). The total protein yield of the synthetic gene was greater than wtα-cgt expression (1,710 mg L⁻¹) by 2,520 mg L⁻¹, with the extracellular enzyme activity being improved to 55.3 U mL⁻¹ in flask fermentation. ΔG values at -3 to +50 of the pelB site of both genes were -19.10 kcal mol⁻¹. Functionally, coα-CGTase was equally as effective as wtα-CGTase in forming α-cyclodextrin (α-CD). These findings suggest that preferred codon usage is advantageous for translational efficiency to increase protein expression. Finally, batch fermentation was applied, and the extracellular coα-CGTase enzyme activity was 326 % that of wtα-CGTase. The results suggest that codon optimization is a reasonable strategy to improve the yield of α-CGTase for industrial application.
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