Publication: Impact of the Expression System on Recombinant Protein Production in Escherichia coli BL21
Authors
Lozano Terol, Gema ; Cánovas Díaz, Manuel ; Diego Puente, Teresa de ; Gallego Jara, Julia ; Martínez Vivancos, Adrián ; Sola Martínez, Rosa Alba
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Publisher
Frontiers Media
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DOI
https://doi.org/10.3389/fmicb.2021.682001
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info:eu-repo/semantics/article
Description
© 2021. The authors. This document is made available under the CC-BY 4.0 license http://creativecommons.org/licenses/by /4.0/
This document is the submitted/accepted/ published version of a Published Work that appeared in final form in Frontiers in Microbiology. To access the final edited and published work see https://doi.org/10.3389/fmicb.2021.682001
Abstract
Recombinant protein production for medical, academic, or industrial applications is essential for our current life. Recombinant proteins are obtained mainly through microbial fermentation, with Escherichia coli being the host most used. In spite of that, some problems are associated with the production of recombinant proteins in E. coli, such as the formation of inclusion bodies, the metabolic burden, or the inefficient translocation/transport system of expressed proteins. Optimizing transcription of heterologous genes is essential to avoid these drawbacks and develop competitive biotechnological processes. Here, expression of YFP reporter protein is evaluated under the control of four promoters of different strength (PT7lac, Ptrc, Ptac, and PBAD) and two different replication origins (high copy number pMB10 and low copy number p15A). In addition, the study has been carried out with the E. coli BL21 wt and the ackA mutant strain growing in a rich medium with glucose or glycerol as carbon sources. Results showed that metabolic burden associated with transcription and translation of foreign genes involves a decrease in recombinant protein expression. It is necessary to find a balance between plasmid copy number and promoter strength to maximize soluble recombinant protein expression. The results obtained represent an important advance on the most suitable expression system to improve both the quantity and quality of recombinant proteins in bioproduction engineering.
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Citation
Frontiers In Microbiology (June 2021) vol. 12, 682001
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