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Impact of cold plasma processing on major peanut allergens
Cold plasma is emerging as a novel food processing technology, with demonstrated efficacies for microbial inactivation and residual chemical dissipation of food products. Given the technology’s multimodal action it has the potential to reduce allergens in foods, however data on the efficacy and mech...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7550356/ https://www.ncbi.nlm.nih.gov/pubmed/33046788 http://dx.doi.org/10.1038/s41598-020-72636-w |
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author | Venkataratnam, Harshitha Cahill, Orla Sarangapani, Chaitanya Cullen, P. J. Barry-Ryan, Catherine |
author_facet | Venkataratnam, Harshitha Cahill, Orla Sarangapani, Chaitanya Cullen, P. J. Barry-Ryan, Catherine |
author_sort | Venkataratnam, Harshitha |
collection | PubMed |
description | Cold plasma is emerging as a novel food processing technology, with demonstrated efficacies for microbial inactivation and residual chemical dissipation of food products. Given the technology’s multimodal action it has the potential to reduce allergens in foods, however data on the efficacy and mechanisms of action are sparse. This study investigates the efficacy of cold plasma on major peanut allergens (Ara h 1 and Ara h 2). For this purpose, dry, whole peanut (WP) and defatted peanut flour (DPF) were subjected to an atmospheric air discharge using a pin to plate cold plasma reactor for different treatment durations. With increases in plasma exposure, SDS-PAGE analysis revealed reduced protein solubility of the major peanut allergens. Alterations in allergenicity and structure of Ara h 1 and Ara h 2 were examined using ELISA and circular dichroism (CD) spectroscopy. Competitive ELISA with proteins purified from plasma treated WP or DPF revealed reduced antigenicity for both Ara h 1 and Ara h 2. The highest reduction in antigenicity was 65% for Ara h 1 and 66% Ara h 2 when purified from DPF. Results from CD spectroscopy analysis of purified proteins strongly suggests the reduction in antigenicity is due to modifications in the secondary structure of the allergens induced by plasma reactive species. Cold plasma is effective at reducing peanut protein solubility and causes changes in allergen structure leading to reduced antigenicity. |
format | Online Article Text |
id | pubmed-7550356 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-75503562020-10-14 Impact of cold plasma processing on major peanut allergens Venkataratnam, Harshitha Cahill, Orla Sarangapani, Chaitanya Cullen, P. J. Barry-Ryan, Catherine Sci Rep Article Cold plasma is emerging as a novel food processing technology, with demonstrated efficacies for microbial inactivation and residual chemical dissipation of food products. Given the technology’s multimodal action it has the potential to reduce allergens in foods, however data on the efficacy and mechanisms of action are sparse. This study investigates the efficacy of cold plasma on major peanut allergens (Ara h 1 and Ara h 2). For this purpose, dry, whole peanut (WP) and defatted peanut flour (DPF) were subjected to an atmospheric air discharge using a pin to plate cold plasma reactor for different treatment durations. With increases in plasma exposure, SDS-PAGE analysis revealed reduced protein solubility of the major peanut allergens. Alterations in allergenicity and structure of Ara h 1 and Ara h 2 were examined using ELISA and circular dichroism (CD) spectroscopy. Competitive ELISA with proteins purified from plasma treated WP or DPF revealed reduced antigenicity for both Ara h 1 and Ara h 2. The highest reduction in antigenicity was 65% for Ara h 1 and 66% Ara h 2 when purified from DPF. Results from CD spectroscopy analysis of purified proteins strongly suggests the reduction in antigenicity is due to modifications in the secondary structure of the allergens induced by plasma reactive species. Cold plasma is effective at reducing peanut protein solubility and causes changes in allergen structure leading to reduced antigenicity. Nature Publishing Group UK 2020-10-12 /pmc/articles/PMC7550356/ /pubmed/33046788 http://dx.doi.org/10.1038/s41598-020-72636-w Text en © The Author(s) 2020 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/. |
spellingShingle | Article Venkataratnam, Harshitha Cahill, Orla Sarangapani, Chaitanya Cullen, P. J. Barry-Ryan, Catherine Impact of cold plasma processing on major peanut allergens |
title | Impact of cold plasma processing on major peanut allergens |
title_full | Impact of cold plasma processing on major peanut allergens |
title_fullStr | Impact of cold plasma processing on major peanut allergens |
title_full_unstemmed | Impact of cold plasma processing on major peanut allergens |
title_short | Impact of cold plasma processing on major peanut allergens |
title_sort | impact of cold plasma processing on major peanut allergens |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7550356/ https://www.ncbi.nlm.nih.gov/pubmed/33046788 http://dx.doi.org/10.1038/s41598-020-72636-w |
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