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Título: | Antibody binding and functional properties of whey protein hydrolysates obtained under high pressure |
Autor: | Chicón, Rosa CSIC; Belloque, Josefina CSIC ORCID; Alonso Prados, Elena CSIC ORCID; López-Fandiño, Rosina CSIC ORCID | Palabras clave: | Whey proteins Hydrolysates High pressure IgG-binding IgE-binding Heat stability Emulsifying activity |
Fecha de publicación: | may-2009 | Editor: | Elsevier | Citación: | Food Hydrocolloids 23(3): 593-599 (2009) | Resumen: | This paper examines the potential of high hydrostatic pressure to produce whey protein hydrolysates that combine low immunoglobulin (Ig)G- and IgE-binding with acceptable functional properties, with the aim to produce milk-based ingredients with reduced potential allergenicity that could be used in hypoallergenic foods. Treatment with pepsin and chymotrypsin under high pressure produced, in minutes, hydrolysates in which α-lactalbumin and β-lactoglobulin were totally proteolysed, giving rise to large and hydrophobic peptides. Such hydrolysates presented reduced antigenicity and human IgE-binding properties. The hydrolysates obtained with pepsin at 400 MPa showed improved heat stability, particularly at a pH, close to the isoelectric point of the whey proteins, and their emulsion activity indexes at pH 7.0 were superior to those of the untreated whey proteins. These results suggest that the peptides present retained low antigenicity together with sufficient capacity to form emulsions. | Descripción: | 7 pages, 4 figures.-- Available online May 18, 2008. | Versión del editor: | http://dx.doi.org/10.1016/j.foodhyd.2008.04.001 | URI: | http://hdl.handle.net/10261/10389 | DOI: | 10.1016/j.foodhyd.2008.04.001 | ISSN: | 0268-005X |
Aparece en las colecciones: | (IFI) Artículos |
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