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Recent contributions in the field of the recombinant expression of disulfide bonded proteins in bacteria
The production of heterologous disulfide bonded proteins in bacteria remains a biotechnological challenge. A rapid literature survey results in the identification of some interesting proposals, such as the option of producing functional proteins in the cytoplasm in the presence of sulfhydryl oxidase...
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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BioMed Central
2012
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3462667/ https://www.ncbi.nlm.nih.gov/pubmed/22978724 http://dx.doi.org/10.1186/1475-2859-11-129 |
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author | de Marco, Ario |
author_facet | de Marco, Ario |
author_sort | de Marco, Ario |
collection | PubMed |
description | The production of heterologous disulfide bonded proteins in bacteria remains a biotechnological challenge. A rapid literature survey results in the identification of some interesting proposals, such as the option of producing functional proteins in the cytoplasm in the presence of sulfhydryl oxidases and isomerases. Furthermore, an ever-increasing number of applications refers to recombinant proteins displayed at the bacterial surface. Time will tell whether these developments will lead to universally accepted laboratory protocols. |
format | Online Article Text |
id | pubmed-3462667 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2012 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-34626672012-10-03 Recent contributions in the field of the recombinant expression of disulfide bonded proteins in bacteria de Marco, Ario Microb Cell Fact Commentary The production of heterologous disulfide bonded proteins in bacteria remains a biotechnological challenge. A rapid literature survey results in the identification of some interesting proposals, such as the option of producing functional proteins in the cytoplasm in the presence of sulfhydryl oxidases and isomerases. Furthermore, an ever-increasing number of applications refers to recombinant proteins displayed at the bacterial surface. Time will tell whether these developments will lead to universally accepted laboratory protocols. BioMed Central 2012-09-14 /pmc/articles/PMC3462667/ /pubmed/22978724 http://dx.doi.org/10.1186/1475-2859-11-129 Text en Copyright ©2012 de Marco; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Commentary de Marco, Ario Recent contributions in the field of the recombinant expression of disulfide bonded proteins in bacteria |
title | Recent contributions in the field of the recombinant expression of disulfide bonded proteins in bacteria |
title_full | Recent contributions in the field of the recombinant expression of disulfide bonded proteins in bacteria |
title_fullStr | Recent contributions in the field of the recombinant expression of disulfide bonded proteins in bacteria |
title_full_unstemmed | Recent contributions in the field of the recombinant expression of disulfide bonded proteins in bacteria |
title_short | Recent contributions in the field of the recombinant expression of disulfide bonded proteins in bacteria |
title_sort | recent contributions in the field of the recombinant expression of disulfide bonded proteins in bacteria |
topic | Commentary |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3462667/ https://www.ncbi.nlm.nih.gov/pubmed/22978724 http://dx.doi.org/10.1186/1475-2859-11-129 |
work_keys_str_mv | AT demarcoario recentcontributionsinthefieldoftherecombinantexpressionofdisulfidebondedproteinsinbacteria |