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Stability and Activity of the Antimicrobial Peptide Leg1 in Solution and on Meat and Its Optimized Generation from Chickpea Storage Protein
The antimicrobial peptide Leg1 (RIKTVTSFDLPALRFLKL) from chickpea legumin is active against spoilage bacteria, yeast, and mold. The present study tested its effectiveness under food storage conditions and examined options to obtain a food-grade agent. The minimum inhibitory concentration (MIC) of Le...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8227015/ https://www.ncbi.nlm.nih.gov/pubmed/34070446 http://dx.doi.org/10.3390/foods10061192 |
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author | Heymich, Marie-Louise Srirangan, Showmika Pischetsrieder, Monika |
author_facet | Heymich, Marie-Louise Srirangan, Showmika Pischetsrieder, Monika |
author_sort | Heymich, Marie-Louise |
collection | PubMed |
description | The antimicrobial peptide Leg1 (RIKTVTSFDLPALRFLKL) from chickpea legumin is active against spoilage bacteria, yeast, and mold. The present study tested its effectiveness under food storage conditions and examined options to obtain a food-grade agent. The minimum inhibitory concentration (MIC) of Leg1 against E. coli (62.5 µM) proved stable over seven days at 20 °C or 4 °C. It was not influenced by reduced pH (5.0 vs. 6.8), which is relevant in food such as meat. An incubation temperature of 20 °C vs. 37 °C reduced the MIC to 15.6/7.8 µM against E. coli/B. subtilis. With a minimum bactericidal concentration in meat of 125/15.6 µM against E. coli/B. subtilis, Leg1 is equivalently effective as nisin and 5000–82,000 times more active than sodium benzoate, potassium sorbate, or sodium nitrite. Replacing the counter-ion trifluoroacetate derived from peptide synthesis by the more natural alternatives acetate or chloride did not impair the activity of Leg1. As an alternative to chemical synthesis, an optimized protocol for chymotryptic hydrolysis was developed, increasing the yield from chickpea legumin by a factor of 30 compared to the standard procedure. The present results indicate that food-grade Leg1 could possibly be applicable for food preservation. |
format | Online Article Text |
id | pubmed-8227015 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-82270152021-06-26 Stability and Activity of the Antimicrobial Peptide Leg1 in Solution and on Meat and Its Optimized Generation from Chickpea Storage Protein Heymich, Marie-Louise Srirangan, Showmika Pischetsrieder, Monika Foods Article The antimicrobial peptide Leg1 (RIKTVTSFDLPALRFLKL) from chickpea legumin is active against spoilage bacteria, yeast, and mold. The present study tested its effectiveness under food storage conditions and examined options to obtain a food-grade agent. The minimum inhibitory concentration (MIC) of Leg1 against E. coli (62.5 µM) proved stable over seven days at 20 °C or 4 °C. It was not influenced by reduced pH (5.0 vs. 6.8), which is relevant in food such as meat. An incubation temperature of 20 °C vs. 37 °C reduced the MIC to 15.6/7.8 µM against E. coli/B. subtilis. With a minimum bactericidal concentration in meat of 125/15.6 µM against E. coli/B. subtilis, Leg1 is equivalently effective as nisin and 5000–82,000 times more active than sodium benzoate, potassium sorbate, or sodium nitrite. Replacing the counter-ion trifluoroacetate derived from peptide synthesis by the more natural alternatives acetate or chloride did not impair the activity of Leg1. As an alternative to chemical synthesis, an optimized protocol for chymotryptic hydrolysis was developed, increasing the yield from chickpea legumin by a factor of 30 compared to the standard procedure. The present results indicate that food-grade Leg1 could possibly be applicable for food preservation. MDPI 2021-05-25 /pmc/articles/PMC8227015/ /pubmed/34070446 http://dx.doi.org/10.3390/foods10061192 Text en © 2021 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Heymich, Marie-Louise Srirangan, Showmika Pischetsrieder, Monika Stability and Activity of the Antimicrobial Peptide Leg1 in Solution and on Meat and Its Optimized Generation from Chickpea Storage Protein |
title | Stability and Activity of the Antimicrobial Peptide Leg1 in Solution and on Meat and Its Optimized Generation from Chickpea Storage Protein |
title_full | Stability and Activity of the Antimicrobial Peptide Leg1 in Solution and on Meat and Its Optimized Generation from Chickpea Storage Protein |
title_fullStr | Stability and Activity of the Antimicrobial Peptide Leg1 in Solution and on Meat and Its Optimized Generation from Chickpea Storage Protein |
title_full_unstemmed | Stability and Activity of the Antimicrobial Peptide Leg1 in Solution and on Meat and Its Optimized Generation from Chickpea Storage Protein |
title_short | Stability and Activity of the Antimicrobial Peptide Leg1 in Solution and on Meat and Its Optimized Generation from Chickpea Storage Protein |
title_sort | stability and activity of the antimicrobial peptide leg1 in solution and on meat and its optimized generation from chickpea storage protein |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8227015/ https://www.ncbi.nlm.nih.gov/pubmed/34070446 http://dx.doi.org/10.3390/foods10061192 |
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