In vitro digestibility of bovine β-casein with simulated and human oral and gastrointestinal fluids. Identification and IgE-reactivity of the resultant peptides
Stability during digestion is considered an important feature in determining the allergenicity of food proteins. This study aimed to provide an immunological characterisation of the digestion products of the major cow's milk allergen β-casein (β-CN) produced by in vitro orogastrointestinal hydrolysis with simulated and human digestive fluids. β-CN was unaffected by oral digestion, but quickly broke down during the early stages of gastric digestion. The degradation with human fluids was faster than that with commercial enzymes. There were similarities in the peptide patterns of the hydrolysates produced in both models, showing 20 peptides in common after gastric digestion. After gastroduodenal digestion, the human fluids gave less numerous and shorter peptides. The IgE binding of most of the individual sera used to the hydrolysates produced with simulated and human fluids increased at the end of the gastric phase and decreased when the duodenal digestion was completed. Two IgE-binding synthetic peptides: β-CN (57-68) and β-CN (82-93), which matched fragments released by β-CN following in vitro digestion with simulated and human fluids, consisted of the most immunoreactive areas of the protein. The similarities found between the in vitro simulated digestion system and that using human digestive fluids suggest that the former would provide a reasonably good estimation of the potential allergenicity of protein digests. © 2013 Elsevier Ltd. All rights reserved.
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Elsevier
2014
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| Subjects: | In vitro digestion, β-Casein, Human digestive fluids, IgE, Peptide microarray, Milk allergy, |
| Online Access: | http://hdl.handle.net/10261/100121 http://dx.doi.org/10.13039/501100000780 http://dx.doi.org/10.13039/501100003339 http://dx.doi.org/10.13039/501100003329 |
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dig-cial-es-10261-1001212018-09-20T07:41:27Z In vitro digestibility of bovine β-casein with simulated and human oral and gastrointestinal fluids. Identification and IgE-reactivity of the resultant peptides Benedé, Sara López-Expósito, Iván Molina, Elena López-Fandiño, Rosina Programa Iberoamericano de Ciencia y Tecnología para el Desarrollo European Commission Consejo Superior de Investigaciones Científicas (España) Ministerio de Economía y Competitividad (España) In vitro digestion β-Casein Human digestive fluids IgE Peptide microarray Milk allergy Stability during digestion is considered an important feature in determining the allergenicity of food proteins. This study aimed to provide an immunological characterisation of the digestion products of the major cow's milk allergen β-casein (β-CN) produced by in vitro orogastrointestinal hydrolysis with simulated and human digestive fluids. β-CN was unaffected by oral digestion, but quickly broke down during the early stages of gastric digestion. The degradation with human fluids was faster than that with commercial enzymes. There were similarities in the peptide patterns of the hydrolysates produced in both models, showing 20 peptides in common after gastric digestion. After gastroduodenal digestion, the human fluids gave less numerous and shorter peptides. The IgE binding of most of the individual sera used to the hydrolysates produced with simulated and human fluids increased at the end of the gastric phase and decreased when the duodenal digestion was completed. Two IgE-binding synthetic peptides: β-CN (57-68) and β-CN (82-93), which matched fragments released by β-CN following in vitro digestion with simulated and human fluids, consisted of the most immunoreactive areas of the protein. The similarities found between the in vitro simulated digestion system and that using human digestive fluids suggest that the former would provide a reasonably good estimation of the potential allergenicity of protein digests. © 2013 Elsevier Ltd. All rights reserved. This work was funded by the project AGL2011-24740. S.B, I.L-E and E.M are participants of COST-Infogest FA 1005 and CYTED-IBEROFUN 110AC0386 projects. S. B and I. L-E acknowledge the financial support of CSIC through JAE Pre and JAE Doc grants. Peer Reviewed 2014-07-18T07:36:52Z 2014-07-18T07:36:52Z 2014 2014-07-18T07:36:53Z artículo http://purl.org/coar/resource_type/c_6501 doi: 10.1016/j.foodchem.2013.07.110 issn: 0308-8146 Food Chemistry 143: 514-521 (2014) http://hdl.handle.net/10261/100121 10.1016/j.foodchem.2013.07.110 http://dx.doi.org/10.13039/501100000780 http://dx.doi.org/10.13039/501100003339 http://dx.doi.org/10.13039/501100003329 Sí none Elsevier |
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In vitro digestion β-Casein Human digestive fluids IgE Peptide microarray Milk allergy In vitro digestion β-Casein Human digestive fluids IgE Peptide microarray Milk allergy |
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In vitro digestion β-Casein Human digestive fluids IgE Peptide microarray Milk allergy In vitro digestion β-Casein Human digestive fluids IgE Peptide microarray Milk allergy Benedé, Sara López-Expósito, Iván Molina, Elena López-Fandiño, Rosina In vitro digestibility of bovine β-casein with simulated and human oral and gastrointestinal fluids. Identification and IgE-reactivity of the resultant peptides |
| description |
Stability during digestion is considered an important feature in determining the allergenicity of food proteins. This study aimed to provide an immunological characterisation of the digestion products of the major cow's milk allergen β-casein (β-CN) produced by in vitro orogastrointestinal hydrolysis with simulated and human digestive fluids. β-CN was unaffected by oral digestion, but quickly broke down during the early stages of gastric digestion. The degradation with human fluids was faster than that with commercial enzymes. There were similarities in the peptide patterns of the hydrolysates produced in both models, showing 20 peptides in common after gastric digestion. After gastroduodenal digestion, the human fluids gave less numerous and shorter peptides. The IgE binding of most of the individual sera used to the hydrolysates produced with simulated and human fluids increased at the end of the gastric phase and decreased when the duodenal digestion was completed. Two IgE-binding synthetic peptides: β-CN (57-68) and β-CN (82-93), which matched fragments released by β-CN following in vitro digestion with simulated and human fluids, consisted of the most immunoreactive areas of the protein. The similarities found between the in vitro simulated digestion system and that using human digestive fluids suggest that the former would provide a reasonably good estimation of the potential allergenicity of protein digests. © 2013 Elsevier Ltd. All rights reserved. |
| author2 |
Programa Iberoamericano de Ciencia y Tecnología para el Desarrollo |
| author_facet |
Programa Iberoamericano de Ciencia y Tecnología para el Desarrollo Benedé, Sara López-Expósito, Iván Molina, Elena López-Fandiño, Rosina |
| format |
artículo |
| topic_facet |
In vitro digestion β-Casein Human digestive fluids IgE Peptide microarray Milk allergy |
| author |
Benedé, Sara López-Expósito, Iván Molina, Elena López-Fandiño, Rosina |
| author_sort |
Benedé, Sara |
| title |
In vitro digestibility of bovine β-casein with simulated and human oral and gastrointestinal fluids. Identification and IgE-reactivity of the resultant peptides |
| title_short |
In vitro digestibility of bovine β-casein with simulated and human oral and gastrointestinal fluids. Identification and IgE-reactivity of the resultant peptides |
| title_full |
In vitro digestibility of bovine β-casein with simulated and human oral and gastrointestinal fluids. Identification and IgE-reactivity of the resultant peptides |
| title_fullStr |
In vitro digestibility of bovine β-casein with simulated and human oral and gastrointestinal fluids. Identification and IgE-reactivity of the resultant peptides |
| title_full_unstemmed |
In vitro digestibility of bovine β-casein with simulated and human oral and gastrointestinal fluids. Identification and IgE-reactivity of the resultant peptides |
| title_sort |
in vitro digestibility of bovine β-casein with simulated and human oral and gastrointestinal fluids. identification and ige-reactivity of the resultant peptides |
| publisher |
Elsevier |
| publishDate |
2014 |
| url |
http://hdl.handle.net/10261/100121 http://dx.doi.org/10.13039/501100000780 http://dx.doi.org/10.13039/501100003339 http://dx.doi.org/10.13039/501100003329 |
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