IgE-Binding and Immunostimulating Properties of Enzymatic Crosslinked Milk Proteins as Influenced by Food Matrix and Digestibility
Dairy foods are essential in the diet, although in some susceptible individuals they may cause allergy to cow’s milk proteins. Therefore, alternative methods are sought to reduce their allergenicity. Transglutaminase (TG) is widely used in dairy products mainly to improve texture. Although it has be...
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| Format: | Article |
| Language: | English |
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MDPI AG
2022-11-01
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| Series: | Nutrients |
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| Online Access: | https://www.mdpi.com/2072-6643/14/21/4584 |
| _version_ | 1797466917661835264 |
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| author | Sara Benedé Mónica Martínez-Blanco Rosina López-Fandiño Elena Molina |
| author_facet | Sara Benedé Mónica Martínez-Blanco Rosina López-Fandiño Elena Molina |
| author_sort | Sara Benedé |
| collection | DOAJ |
| description | Dairy foods are essential in the diet, although in some susceptible individuals they may cause allergy to cow’s milk proteins. Therefore, alternative methods are sought to reduce their allergenicity. Transglutaminase (TG) is widely used in dairy products mainly to improve texture. Although it has been claimed that TG can be used to modify the digestibility and allergenicity of foods, its impact within a real matrix has been rarely studied. The aim of this work was to assess the allergenic potential of crosslinked skim milk (SM), milk casein fraction (CN), and whey protein (WP). To this purpose, inhibition ELISA with sera from milk allergic patients, in vitro activation tests of mouse mast cells and splenocytes, and simulated gastrointestinal digestion assays were performed. The results showed that cross-linking increased the binding of IgE to WP, but decreased IgE-binding to SM and CN. However, no differences were observed in the ability of cross-linked proteins to induce mast cell degranulation compared to native proteins. The cross-linking of SM and CN reduced Th2 cytokine release from the splenocytes of sensitized mice. All TG-treated samples exhibited more resistance to in vitro digestion than the untreated proteins and the human IgE binding capacity after digestion was higher. In conclusion, TG treatment of milk proteins does not reduce the risk of eliciting allergic symptoms in cow’s milk allergic patients. |
| first_indexed | 2024-03-09T18:46:15Z |
| format | Article |
| id | doaj.art-a80616d8a6d1492f9df5ad1d2a44e00f |
| institution | Directory Open Access Journal |
| issn | 2072-6643 |
| language | English |
| last_indexed | 2024-03-09T18:46:15Z |
| publishDate | 2022-11-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Nutrients |
| spelling | doaj.art-a80616d8a6d1492f9df5ad1d2a44e00f2023-11-24T06:13:53ZengMDPI AGNutrients2072-66432022-11-011421458410.3390/nu14214584IgE-Binding and Immunostimulating Properties of Enzymatic Crosslinked Milk Proteins as Influenced by Food Matrix and DigestibilitySara Benedé0Mónica Martínez-Blanco1Rosina López-Fandiño2Elena Molina3Instituto de Investigación en Ciencias de la Alimentación (CIAL, CSIC-UAM), Nicolás Cabrera 9, 28049 Madrid, SpainInstituto de Investigación en Ciencias de la Alimentación (CIAL, CSIC-UAM), Nicolás Cabrera 9, 28049 Madrid, SpainInstituto de Investigación en Ciencias de la Alimentación (CIAL, CSIC-UAM), Nicolás Cabrera 9, 28049 Madrid, SpainInstituto de Investigación en Ciencias de la Alimentación (CIAL, CSIC-UAM), Nicolás Cabrera 9, 28049 Madrid, SpainDairy foods are essential in the diet, although in some susceptible individuals they may cause allergy to cow’s milk proteins. Therefore, alternative methods are sought to reduce their allergenicity. Transglutaminase (TG) is widely used in dairy products mainly to improve texture. Although it has been claimed that TG can be used to modify the digestibility and allergenicity of foods, its impact within a real matrix has been rarely studied. The aim of this work was to assess the allergenic potential of crosslinked skim milk (SM), milk casein fraction (CN), and whey protein (WP). To this purpose, inhibition ELISA with sera from milk allergic patients, in vitro activation tests of mouse mast cells and splenocytes, and simulated gastrointestinal digestion assays were performed. The results showed that cross-linking increased the binding of IgE to WP, but decreased IgE-binding to SM and CN. However, no differences were observed in the ability of cross-linked proteins to induce mast cell degranulation compared to native proteins. The cross-linking of SM and CN reduced Th2 cytokine release from the splenocytes of sensitized mice. All TG-treated samples exhibited more resistance to in vitro digestion than the untreated proteins and the human IgE binding capacity after digestion was higher. In conclusion, TG treatment of milk proteins does not reduce the risk of eliciting allergic symptoms in cow’s milk allergic patients.https://www.mdpi.com/2072-6643/14/21/4584milk allergenscaseinwhey proteintransglutaminaseallergenicitydigestion |
| spellingShingle | Sara Benedé Mónica Martínez-Blanco Rosina López-Fandiño Elena Molina IgE-Binding and Immunostimulating Properties of Enzymatic Crosslinked Milk Proteins as Influenced by Food Matrix and Digestibility Nutrients milk allergens casein whey protein transglutaminase allergenicity digestion |
| title | IgE-Binding and Immunostimulating Properties of Enzymatic Crosslinked Milk Proteins as Influenced by Food Matrix and Digestibility |
| title_full | IgE-Binding and Immunostimulating Properties of Enzymatic Crosslinked Milk Proteins as Influenced by Food Matrix and Digestibility |
| title_fullStr | IgE-Binding and Immunostimulating Properties of Enzymatic Crosslinked Milk Proteins as Influenced by Food Matrix and Digestibility |
| title_full_unstemmed | IgE-Binding and Immunostimulating Properties of Enzymatic Crosslinked Milk Proteins as Influenced by Food Matrix and Digestibility |
| title_short | IgE-Binding and Immunostimulating Properties of Enzymatic Crosslinked Milk Proteins as Influenced by Food Matrix and Digestibility |
| title_sort | ige binding and immunostimulating properties of enzymatic crosslinked milk proteins as influenced by food matrix and digestibility |
| topic | milk allergens casein whey protein transglutaminase allergenicity digestion |
| url | https://www.mdpi.com/2072-6643/14/21/4584 |
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