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The Impact of Processing and Extraction Methods on the Allergenicity of Targeted Protein Quantification as Well as Bioactive Peptides Derived from Egg
This review article discusses advanced extraction methods to enhance the functionality of egg-derived peptides while reducing their allergenicity. While eggs are considered a nutrient-dense food, some proteins can cause allergic reactions in susceptible individuals. Therefore, various methods have b...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2023
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10053729/ https://www.ncbi.nlm.nih.gov/pubmed/36985630 http://dx.doi.org/10.3390/molecules28062658 |
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author | Mostashari, Parisa Marszałek, Krystian Aliyeva, Aynura Mousavi Khaneghah, Amin |
author_facet | Mostashari, Parisa Marszałek, Krystian Aliyeva, Aynura Mousavi Khaneghah, Amin |
author_sort | Mostashari, Parisa |
collection | PubMed |
description | This review article discusses advanced extraction methods to enhance the functionality of egg-derived peptides while reducing their allergenicity. While eggs are considered a nutrient-dense food, some proteins can cause allergic reactions in susceptible individuals. Therefore, various methods have been developed to reduce the allergenicity of egg-derived proteins, such as enzymatic hydrolysis, heat treatment, and glycosylation. In addition to reducing allergenicity, advanced extraction methods can enhance the functionality of egg-derived peptides. Techniques such as membrane separation, chromatography, and electrodialysis can isolate and purify specific egg-derived peptides with desired functional properties, improving their bioactivity. Further, enzymatic hydrolysis can also break down polypeptide sequences and produce bioactive peptides with various health benefits. While liquid chromatography is the most commonly used method to obtain individual proteins for developing novel food products, several challenges are associated with optimizing extraction conditions to maximize functionality and allergenicity reduction. The article also highlights the challenges and future perspectives, including optimizing extraction conditions to maximize functionality and allergenicity reduction. The review concludes by highlighting the potential for future research in this area to improve the safety and efficacy of egg-derived peptides more broadly. |
format | Online Article Text |
id | pubmed-10053729 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-100537292023-03-30 The Impact of Processing and Extraction Methods on the Allergenicity of Targeted Protein Quantification as Well as Bioactive Peptides Derived from Egg Mostashari, Parisa Marszałek, Krystian Aliyeva, Aynura Mousavi Khaneghah, Amin Molecules Review This review article discusses advanced extraction methods to enhance the functionality of egg-derived peptides while reducing their allergenicity. While eggs are considered a nutrient-dense food, some proteins can cause allergic reactions in susceptible individuals. Therefore, various methods have been developed to reduce the allergenicity of egg-derived proteins, such as enzymatic hydrolysis, heat treatment, and glycosylation. In addition to reducing allergenicity, advanced extraction methods can enhance the functionality of egg-derived peptides. Techniques such as membrane separation, chromatography, and electrodialysis can isolate and purify specific egg-derived peptides with desired functional properties, improving their bioactivity. Further, enzymatic hydrolysis can also break down polypeptide sequences and produce bioactive peptides with various health benefits. While liquid chromatography is the most commonly used method to obtain individual proteins for developing novel food products, several challenges are associated with optimizing extraction conditions to maximize functionality and allergenicity reduction. The article also highlights the challenges and future perspectives, including optimizing extraction conditions to maximize functionality and allergenicity reduction. The review concludes by highlighting the potential for future research in this area to improve the safety and efficacy of egg-derived peptides more broadly. MDPI 2023-03-15 /pmc/articles/PMC10053729/ /pubmed/36985630 http://dx.doi.org/10.3390/molecules28062658 Text en © 2023 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 | Review Mostashari, Parisa Marszałek, Krystian Aliyeva, Aynura Mousavi Khaneghah, Amin The Impact of Processing and Extraction Methods on the Allergenicity of Targeted Protein Quantification as Well as Bioactive Peptides Derived from Egg |
title | The Impact of Processing and Extraction Methods on the Allergenicity of Targeted Protein Quantification as Well as Bioactive Peptides Derived from Egg |
title_full | The Impact of Processing and Extraction Methods on the Allergenicity of Targeted Protein Quantification as Well as Bioactive Peptides Derived from Egg |
title_fullStr | The Impact of Processing and Extraction Methods on the Allergenicity of Targeted Protein Quantification as Well as Bioactive Peptides Derived from Egg |
title_full_unstemmed | The Impact of Processing and Extraction Methods on the Allergenicity of Targeted Protein Quantification as Well as Bioactive Peptides Derived from Egg |
title_short | The Impact of Processing and Extraction Methods on the Allergenicity of Targeted Protein Quantification as Well as Bioactive Peptides Derived from Egg |
title_sort | impact of processing and extraction methods on the allergenicity of targeted protein quantification as well as bioactive peptides derived from egg |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10053729/ https://www.ncbi.nlm.nih.gov/pubmed/36985630 http://dx.doi.org/10.3390/molecules28062658 |
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