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Insights into the Mechanism Underlying the Influence of Glycation with Different Saccharides and Temperatures on the IgG/IgE Binding Ability, Immunodetection, In Vitro Digestibility of Shrimp (Litopenaeus vannamei) Tropomyosin
Tropomyosin (TM) is a heat-stable protein that plays a crucial role as a major pan-allergen in crustacean shellfish. Despite the high thermal stability of the TM structure, its IgG/IgE binding ability, immunodetection, and in vitro digestibility can be negatively influenced by glycation during food...
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/PMC10453262/ https://www.ncbi.nlm.nih.gov/pubmed/37628047 http://dx.doi.org/10.3390/foods12163049 |
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author | Zhao, Jinlong Wang, Jin Xu, Lili Wang, Hao Zhang, Ziye Lin, Hong Li, Zhenxing |
author_facet | Zhao, Jinlong Wang, Jin Xu, Lili Wang, Hao Zhang, Ziye Lin, Hong Li, Zhenxing |
author_sort | Zhao, Jinlong |
collection | PubMed |
description | Tropomyosin (TM) is a heat-stable protein that plays a crucial role as a major pan-allergen in crustacean shellfish. Despite the high thermal stability of the TM structure, its IgG/IgE binding ability, immunodetection, and in vitro digestibility can be negatively influenced by glycation during food processing, and the underlying mechanism remains unclear. In this study, TM was subjected to glycosylation using various sugars and temperatures. The resulting effects on IgG/IgE-binding capacity, immunodetection, and in vitro digestibility were analyzed, meanwhile, the structural alterations and modifications using spectroscopic and LC-MS/MS analysis were determined. Obtained results suggested that the IgG/IgE binding capacity of glycosylated TM, immunodetection recovery, and in vitro digestibility were significantly reduced depending on the degree of glycosylation, with the greatest reduction occurring in Rib-TM. These changes may be attributable to structural alterations and modifications that occur during glycosylation processing, which could mask or shield antigenic epitopes of TM (E3: 61–81, E5b: 142–162, and E5c: 157–183), subsequently reducing the immunodetection recognition and digestive enzyme degradation. Overall, these findings shed light on the detrimental impact of glycation on TMs potential allergenicity and digestibility immunodetection and provide insights into the structural changes and modifications induced by thermal processing. |
format | Online Article Text |
id | pubmed-10453262 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-104532622023-08-26 Insights into the Mechanism Underlying the Influence of Glycation with Different Saccharides and Temperatures on the IgG/IgE Binding Ability, Immunodetection, In Vitro Digestibility of Shrimp (Litopenaeus vannamei) Tropomyosin Zhao, Jinlong Wang, Jin Xu, Lili Wang, Hao Zhang, Ziye Lin, Hong Li, Zhenxing Foods Article Tropomyosin (TM) is a heat-stable protein that plays a crucial role as a major pan-allergen in crustacean shellfish. Despite the high thermal stability of the TM structure, its IgG/IgE binding ability, immunodetection, and in vitro digestibility can be negatively influenced by glycation during food processing, and the underlying mechanism remains unclear. In this study, TM was subjected to glycosylation using various sugars and temperatures. The resulting effects on IgG/IgE-binding capacity, immunodetection, and in vitro digestibility were analyzed, meanwhile, the structural alterations and modifications using spectroscopic and LC-MS/MS analysis were determined. Obtained results suggested that the IgG/IgE binding capacity of glycosylated TM, immunodetection recovery, and in vitro digestibility were significantly reduced depending on the degree of glycosylation, with the greatest reduction occurring in Rib-TM. These changes may be attributable to structural alterations and modifications that occur during glycosylation processing, which could mask or shield antigenic epitopes of TM (E3: 61–81, E5b: 142–162, and E5c: 157–183), subsequently reducing the immunodetection recognition and digestive enzyme degradation. Overall, these findings shed light on the detrimental impact of glycation on TMs potential allergenicity and digestibility immunodetection and provide insights into the structural changes and modifications induced by thermal processing. MDPI 2023-08-14 /pmc/articles/PMC10453262/ /pubmed/37628047 http://dx.doi.org/10.3390/foods12163049 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 | Article Zhao, Jinlong Wang, Jin Xu, Lili Wang, Hao Zhang, Ziye Lin, Hong Li, Zhenxing Insights into the Mechanism Underlying the Influence of Glycation with Different Saccharides and Temperatures on the IgG/IgE Binding Ability, Immunodetection, In Vitro Digestibility of Shrimp (Litopenaeus vannamei) Tropomyosin |
title | Insights into the Mechanism Underlying the Influence of Glycation with Different Saccharides and Temperatures on the IgG/IgE Binding Ability, Immunodetection, In Vitro Digestibility of Shrimp (Litopenaeus vannamei) Tropomyosin |
title_full | Insights into the Mechanism Underlying the Influence of Glycation with Different Saccharides and Temperatures on the IgG/IgE Binding Ability, Immunodetection, In Vitro Digestibility of Shrimp (Litopenaeus vannamei) Tropomyosin |
title_fullStr | Insights into the Mechanism Underlying the Influence of Glycation with Different Saccharides and Temperatures on the IgG/IgE Binding Ability, Immunodetection, In Vitro Digestibility of Shrimp (Litopenaeus vannamei) Tropomyosin |
title_full_unstemmed | Insights into the Mechanism Underlying the Influence of Glycation with Different Saccharides and Temperatures on the IgG/IgE Binding Ability, Immunodetection, In Vitro Digestibility of Shrimp (Litopenaeus vannamei) Tropomyosin |
title_short | Insights into the Mechanism Underlying the Influence of Glycation with Different Saccharides and Temperatures on the IgG/IgE Binding Ability, Immunodetection, In Vitro Digestibility of Shrimp (Litopenaeus vannamei) Tropomyosin |
title_sort | insights into the mechanism underlying the influence of glycation with different saccharides and temperatures on the igg/ige binding ability, immunodetection, in vitro digestibility of shrimp (litopenaeus vannamei) tropomyosin |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10453262/ https://www.ncbi.nlm.nih.gov/pubmed/37628047 http://dx.doi.org/10.3390/foods12163049 |
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