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Hexametaphosphate, a Common Food Additive, Aggregated the Hen Egg White Lysozyme
[Image: see text] Polyphosphate polymers are chains of phosphate monomers chemically bonded together via phosphoanhydride bonds. They are found in all prokaryotic and eukaryotic organisms and are among the earliest, most anionic, and most mysterious molecules known. They are everywhere, from small c...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Chemical Society
2023
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10666150/ https://www.ncbi.nlm.nih.gov/pubmed/38027328 http://dx.doi.org/10.1021/acsomega.3c06210 |
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author | Malik, Ajamaluddin Khan, Javed Masood Al-Amri, Abdulaziz M. Altwaijry, Nojood Sharma, Prerna Alhomida, Abdullah Sen, Priyankar |
author_facet | Malik, Ajamaluddin Khan, Javed Masood Al-Amri, Abdulaziz M. Altwaijry, Nojood Sharma, Prerna Alhomida, Abdullah Sen, Priyankar |
author_sort | Malik, Ajamaluddin |
collection | PubMed |
description | [Image: see text] Polyphosphate polymers are chains of phosphate monomers chemically bonded together via phosphoanhydride bonds. They are found in all prokaryotic and eukaryotic organisms and are among the earliest, most anionic, and most mysterious molecules known. They are everywhere, from small cellular components to additives in our food. There is a strong association between hyperphosphatemia and mortality. That is why it is crucial to assess how polyphosphates, as food additives, affect the quality of edible proteins. This study investigated the effect of inexpensive and widely used food additives (hexametaphosphate labeled as E452) on bakery items, meat products, fish, and soft drinks. Using various spectroscopic and microscopic techniques, we examined how hexametaphosphate affected the aggregation propensity, structure, and stability of a commonly used food protein: hen egg white lysozyme (HEWL). The solubility of HEWL is affected in a bimodal fashion by the concentration of hexametaphosphate. The bimodal concentration-dependent effect was also observed in the tertiary and secondary structural changes. Hexametaphosphate-induced HEWL aggregates were amorphous, as evidenced by ThT fluorescence, far-UV CD, and TEM imaging. This study showed that the food additive (hexametaphosphate) may denature and aggregate proteins and may lead to undesirable health issues. |
format | Online Article Text |
id | pubmed-10666150 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | American Chemical Society |
record_format | MEDLINE/PubMed |
spelling | pubmed-106661502023-11-10 Hexametaphosphate, a Common Food Additive, Aggregated the Hen Egg White Lysozyme Malik, Ajamaluddin Khan, Javed Masood Al-Amri, Abdulaziz M. Altwaijry, Nojood Sharma, Prerna Alhomida, Abdullah Sen, Priyankar ACS Omega [Image: see text] Polyphosphate polymers are chains of phosphate monomers chemically bonded together via phosphoanhydride bonds. They are found in all prokaryotic and eukaryotic organisms and are among the earliest, most anionic, and most mysterious molecules known. They are everywhere, from small cellular components to additives in our food. There is a strong association between hyperphosphatemia and mortality. That is why it is crucial to assess how polyphosphates, as food additives, affect the quality of edible proteins. This study investigated the effect of inexpensive and widely used food additives (hexametaphosphate labeled as E452) on bakery items, meat products, fish, and soft drinks. Using various spectroscopic and microscopic techniques, we examined how hexametaphosphate affected the aggregation propensity, structure, and stability of a commonly used food protein: hen egg white lysozyme (HEWL). The solubility of HEWL is affected in a bimodal fashion by the concentration of hexametaphosphate. The bimodal concentration-dependent effect was also observed in the tertiary and secondary structural changes. Hexametaphosphate-induced HEWL aggregates were amorphous, as evidenced by ThT fluorescence, far-UV CD, and TEM imaging. This study showed that the food additive (hexametaphosphate) may denature and aggregate proteins and may lead to undesirable health issues. American Chemical Society 2023-11-10 /pmc/articles/PMC10666150/ /pubmed/38027328 http://dx.doi.org/10.1021/acsomega.3c06210 Text en © 2023 The Authors. Published by American Chemical Society https://creativecommons.org/licenses/by-nc-nd/4.0/Permits non-commercial access and re-use, provided that author attribution and integrity are maintained; but does not permit creation of adaptations or other derivative works (https://creativecommons.org/licenses/by-nc-nd/4.0/). |
spellingShingle | Malik, Ajamaluddin Khan, Javed Masood Al-Amri, Abdulaziz M. Altwaijry, Nojood Sharma, Prerna Alhomida, Abdullah Sen, Priyankar Hexametaphosphate, a Common Food Additive, Aggregated the Hen Egg White Lysozyme |
title | Hexametaphosphate,
a Common Food Additive, Aggregated
the Hen Egg White Lysozyme |
title_full | Hexametaphosphate,
a Common Food Additive, Aggregated
the Hen Egg White Lysozyme |
title_fullStr | Hexametaphosphate,
a Common Food Additive, Aggregated
the Hen Egg White Lysozyme |
title_full_unstemmed | Hexametaphosphate,
a Common Food Additive, Aggregated
the Hen Egg White Lysozyme |
title_short | Hexametaphosphate,
a Common Food Additive, Aggregated
the Hen Egg White Lysozyme |
title_sort | hexametaphosphate,
a common food additive, aggregated
the hen egg white lysozyme |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10666150/ https://www.ncbi.nlm.nih.gov/pubmed/38027328 http://dx.doi.org/10.1021/acsomega.3c06210 |
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