English   español  
Por favor, use este identificador para citar o enlazar a este item: http://hdl.handle.net/10261/100058
Compartir / Impacto:
Estadísticas
Add this article to your Mendeley library MendeleyBASE
Citado 14 veces en Web of Knowledge®  |  Pub MebCentral Ver citas en PubMed Central  |  Ver citas en Google académico
Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL
Exportar otros formatos: Exportar EndNote (RIS)Exportar EndNote (RIS)Exportar EndNote (RIS)
Título

Immunological behavior of in vitro digested egg-white lysozyme

Autor Jiménez Saiz, Rodrigo ; Benedé, Sara ; Miralles, Beatriz ; López-Expósito, Iván ; Molina, Elena ; López-Fandiño, Rosina
Palabras clave PBMC stimulation
IgE binding
Gastrointestinal digestion
Egg allergy
Lysozyme
Fecha de publicación 2014
EditorWiley-VCH
Citación Molecular Nutrition and Food Research 58(3): 614-624 (2014)
Resumen[Scope]: Besides its antimicrobial properties, lysozyme (LYS) is one of the major allergens from hen egg. This paper addresses the identification of the peptides produced upon in vitro gastrointestinal digestion of LYS, together with their IgE-binding and biological activity as a contribution to the understanding of what makes it a relevant allergen. [Methods and results]: Simulated in vitro gastrointestinal digestion together with IgE binding, basophil degranulation, and peripheral blood mononuclear cells stimulation experiments were carried out. Identification of the fragments released was performed by HPLC-MS/MS and the immunoreactive products were analyzed by MALDI-TOF/TOF. Results showed that in vitro gastric and gastroduodenal digests of LYS maintained IgE binding, basophil activation capacity, and preserved T-cell immunogenicity. These biological activities could be attributed to either the persistence of intact LYS, due to incomplete gastric degradation and subsequent duodenal precipitation, the formation of fragment f(24-129) by chymotrypsin action on the soluble intact protein, or the release, upon combined gastric and pancreatic digestion, of immunoreactive peptides linked by disulphide bonds containing the epitopes f(57-83) and f(108-122). [Conclusion]: The pH of gastric hydrolysis greatly determined the extent of subsequent duodenal digestion of LYS and the disclosure of relevant epitopes that could increase its allergenic potential. © 2013 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
URI http://hdl.handle.net/10261/100058
DOI10.1002/mnfr.201300442
Identificadoresdoi: 10.1002/mnfr.201300442
issn: 1613-4125
e-issn: 1613-4133
Aparece en las colecciones: (CIAL) Artículos
Ficheros en este ítem:
Fichero Descripción Tamaño Formato  
accesoRestringido.pdf15,38 kBAdobe PDFVista previa
Visualizar/Abrir
Mostrar el registro completo
 



NOTA: Los ítems de Digital.CSIC están protegidos por copyright, con todos los derechos reservados, a menos que se indique lo contrario.