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Impact of the Expression System on Recombinant Protein Production in Escherichia coli BL21

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dc.contributor.authorLozano Terol, Gema
dc.contributor.authorCánovas Díaz, Manuel
dc.contributor.authorDiego Puente, Teresa de
dc.contributor.authorGallego Jara, Julia
dc.contributor.authorMartínez Vivancos, Adrián
dc.contributor.authorSola Martínez, Rosa Alba
dc.contributor.departmentBioquímica y Biología Molecular B e Inmunología
dc.date.accessioned2023-12-12T23:11:50Z
dc.date.available2023-12-12T23:11:50Z
dc.date.issued2021-06-21
dc.description©2021. This manuscript version is made available under the CC-BY 4.0 license http://creativecommons.org/licenses/by /4.0/ This document is the 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
dc.description.abstractRecombinant 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.
dc.formatapplication/pdfes_ES
dc.format.extent12
dc.identifier.citationFrontiers In Microbiology, Volume 12 - Article 682001
dc.identifier.doihttps://doi.org/10.3389/fmicb.2021.682001
dc.identifier.issn1664-302X
dc.identifier.urihttp://hdl.handle.net/10201/136569
dc.languageenges_ES
dc.relation.isreferencedbyED_IDENTRADA=1260
dc.relation.publisherversionhttps://www.frontiersin.org/articles/10.3389/fmicb.2021.682001/full
dc.rightsinfo:eu-repo/semantics/openAccess*
dc.rightsAtribución 4.0 Internacional*
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/*
dc.subjectEscherichia coli
dc.subjectRecombinant protein
dc.subjectExpression system
dc.subjectPromoter
dc.subjectOrigin of replication
dc.subjectMicrobial factory
dc.titleImpact of the Expression System on Recombinant Protein Production in Escherichia coli BL21es_ES
dc.typeinfo:eu-repo/semantics/articlees_ES
dspace.entity.typePublicationes
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relation.isAuthorOfPublication.latestForDiscovery57bf3537-1124-49ab-8774-bd0c3bdf1c28
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