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Expression of bacteriocin divercin AS7 in Escherichia coli and its functional analysis
Bacteriocins are small peptides with antimicrobial activity, that are produced by bacteria. Four classes of bacteriocins produced by lactic acid bacteria have been defined. Class IIa bacteriocins are promising candidates for industrial applications due to their high biological activity and their phy...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Springer Berlin Heidelberg
2013
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4119584/ https://www.ncbi.nlm.nih.gov/pubmed/25100927 http://dx.doi.org/10.1007/s13213-013-0759-x |
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author | Olejnik-Schmidt, Agnieszka K. Schmidt, Marcin T. Sip, Anna Szablewski, Tomasz Grajek, Włodzimierz |
author_facet | Olejnik-Schmidt, Agnieszka K. Schmidt, Marcin T. Sip, Anna Szablewski, Tomasz Grajek, Włodzimierz |
author_sort | Olejnik-Schmidt, Agnieszka K. |
collection | PubMed |
description | Bacteriocins are small peptides with antimicrobial activity, that are produced by bacteria. Four classes of bacteriocins produced by lactic acid bacteria have been defined. Class IIa bacteriocins are promising candidates for industrial applications due to their high biological activity and their physicochemical properties. Divercin AS7 is a class IIa bacteriocin produced by Carnobacterium divergens AS7. It shows antibacterial activity against pathogens and food spoilage flora including Listeria spp. Little is known about the impact of class IIa bacteriocins upon eukaryotic cells. The safe use of bacteriocins as food biopreservatives requires the absence of cytotoxicity to human cells. To analyze the impact of divercin AS7 on human enterocytes, we expressed the recombinant divercin AS7 in the Escherichia coli BL21DE3pLys strain and conducted in vitro studies to evaluate the safety of recombinant divercin AS7. No cytotoxic effect on differentiated monolayer Caco-2 cells and no apoptotic appearance were observed when recombinant divercin AS7 was used at a concentration of 2 μg ml(−1). In our study, divercin AS7 also did not interfere with differentiated Caco-2 cells monolayer integrity. The obtained results suggest that divercin AS7 is a promising peptide for the food industry. |
format | Online Article Text |
id | pubmed-4119584 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
publisher | Springer Berlin Heidelberg |
record_format | MEDLINE/PubMed |
spelling | pubmed-41195842014-08-04 Expression of bacteriocin divercin AS7 in Escherichia coli and its functional analysis Olejnik-Schmidt, Agnieszka K. Schmidt, Marcin T. Sip, Anna Szablewski, Tomasz Grajek, Włodzimierz Ann Microbiol Original Article Bacteriocins are small peptides with antimicrobial activity, that are produced by bacteria. Four classes of bacteriocins produced by lactic acid bacteria have been defined. Class IIa bacteriocins are promising candidates for industrial applications due to their high biological activity and their physicochemical properties. Divercin AS7 is a class IIa bacteriocin produced by Carnobacterium divergens AS7. It shows antibacterial activity against pathogens and food spoilage flora including Listeria spp. Little is known about the impact of class IIa bacteriocins upon eukaryotic cells. The safe use of bacteriocins as food biopreservatives requires the absence of cytotoxicity to human cells. To analyze the impact of divercin AS7 on human enterocytes, we expressed the recombinant divercin AS7 in the Escherichia coli BL21DE3pLys strain and conducted in vitro studies to evaluate the safety of recombinant divercin AS7. No cytotoxic effect on differentiated monolayer Caco-2 cells and no apoptotic appearance were observed when recombinant divercin AS7 was used at a concentration of 2 μg ml(−1). In our study, divercin AS7 also did not interfere with differentiated Caco-2 cells monolayer integrity. The obtained results suggest that divercin AS7 is a promising peptide for the food industry. Springer Berlin Heidelberg 2013-11-27 2014 /pmc/articles/PMC4119584/ /pubmed/25100927 http://dx.doi.org/10.1007/s13213-013-0759-x Text en © The Author(s) 2013 https://creativecommons.org/licenses/by/2.0/ Open Access This article is distributed under the terms of the Creative Commons Attribution License which permits any use, distribution, and reproduction in any medium, provided the original author(s) and the source are credited. |
spellingShingle | Original Article Olejnik-Schmidt, Agnieszka K. Schmidt, Marcin T. Sip, Anna Szablewski, Tomasz Grajek, Włodzimierz Expression of bacteriocin divercin AS7 in Escherichia coli and its functional analysis |
title | Expression of bacteriocin divercin AS7 in Escherichia coli and its functional analysis |
title_full | Expression of bacteriocin divercin AS7 in Escherichia coli and its functional analysis |
title_fullStr | Expression of bacteriocin divercin AS7 in Escherichia coli and its functional analysis |
title_full_unstemmed | Expression of bacteriocin divercin AS7 in Escherichia coli and its functional analysis |
title_short | Expression of bacteriocin divercin AS7 in Escherichia coli and its functional analysis |
title_sort | expression of bacteriocin divercin as7 in escherichia coli and its functional analysis |
topic | Original Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4119584/ https://www.ncbi.nlm.nih.gov/pubmed/25100927 http://dx.doi.org/10.1007/s13213-013-0759-x |
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