Easy and Rapid Purification of Highly Active Nisin

Nisin is an antimicrobial peptide produced and secreted by several L. lactis strains and is specifically active against Gram-positive bacteria. In previous studies, nisin was purified via cation exchange chromatography at low pH employing a single-step elution using 1 M NaCl. Here, we describe an op...

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Autores principales: Abts, André, Mavaro, Antonino, Stindt, Jan, Bakkes, Patrick J., Metzger, Sabine, Driessen, Arnold J. M., Smits, Sander H. J., Schmitt, Lutz
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Hindawi Publishing Corporation 2011
Materias:
Research Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3175705/
https://www.ncbi.nlm.nih.gov/pubmed/21941571
http://dx.doi.org/10.1155/2011/175145
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author Abts, André
Mavaro, Antonino
Stindt, Jan
Bakkes, Patrick J.
Metzger, Sabine
Driessen, Arnold J. M.
Smits, Sander H. J.
Schmitt, Lutz
author_facet Abts, André
Mavaro, Antonino
Stindt, Jan
Bakkes, Patrick J.
Metzger, Sabine
Driessen, Arnold J. M.
Smits, Sander H. J.
Schmitt, Lutz
author_sort Abts, André
collection PubMed
description Nisin is an antimicrobial peptide produced and secreted by several L. lactis strains and is specifically active against Gram-positive bacteria. In previous studies, nisin was purified via cation exchange chromatography at low pH employing a single-step elution using 1 M NaCl. Here, we describe an optimized purification protocol using a five-step NaCl elution to remove contaminants. The obtained nisin is devoid of impurities and shows high bactericidal activity against the nisin-sensitive L. lactis strain NZ9000. Purified nisin exhibits an IC(50) of ~3 nM, which is a tenfold improvement as compared to nisin obtained via the one-step elution procedure.
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spelling pubmed-31757052011-09-22 Easy and Rapid Purification of Highly Active Nisin Abts, André Mavaro, Antonino Stindt, Jan Bakkes, Patrick J. Metzger, Sabine Driessen, Arnold J. M. Smits, Sander H. J. Schmitt, Lutz Int J Pept Research Article Nisin is an antimicrobial peptide produced and secreted by several L. lactis strains and is specifically active against Gram-positive bacteria. In previous studies, nisin was purified via cation exchange chromatography at low pH employing a single-step elution using 1 M NaCl. Here, we describe an optimized purification protocol using a five-step NaCl elution to remove contaminants. The obtained nisin is devoid of impurities and shows high bactericidal activity against the nisin-sensitive L. lactis strain NZ9000. Purified nisin exhibits an IC(50) of ~3 nM, which is a tenfold improvement as compared to nisin obtained via the one-step elution procedure. Hindawi Publishing Corporation 2011 2011-09-18 /pmc/articles/PMC3175705/ /pubmed/21941571 http://dx.doi.org/10.1155/2011/175145 Text en Copyright © 2011 André Abts et al. https://creativecommons.org/licenses/by/3.0/ This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research Article
Abts, André
Mavaro, Antonino
Stindt, Jan
Bakkes, Patrick J.
Metzger, Sabine
Driessen, Arnold J. M.
Smits, Sander H. J.
Schmitt, Lutz
Easy and Rapid Purification of Highly Active Nisin
title Easy and Rapid Purification of Highly Active Nisin
title_full Easy and Rapid Purification of Highly Active Nisin
title_fullStr Easy and Rapid Purification of Highly Active Nisin
title_full_unstemmed Easy and Rapid Purification of Highly Active Nisin
title_short Easy and Rapid Purification of Highly Active Nisin
title_sort easy and rapid purification of highly active nisin
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3175705/
https://www.ncbi.nlm.nih.gov/pubmed/21941571
http://dx.doi.org/10.1155/2011/175145
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