부산대학교 도서관

To link to full-text access for this article, visit this link: http://dx.doi.org/10.1016/j.foodhyd.2008.04.001 Byline: Rosa Chicon (a), Josefina Belloque (a), Elena Alonso (b), Rosina Lopez-FandiA[+ or -]o (a) Abstract: 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 [alpha]-lactalbumin and [beta]-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 400MPa 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. Author Affiliation: (a) Instituto de Fermentaciones Industriales (CSIC), Juan de la Cierva 3, 28006 Madrid, Spain (b) Hospital General Universitario Gregorio MaraA[+ or -]on, Doctor Esquerdo 46, 28007 Madrid, Spain Article History: Received 3 March 2008; Accepted 28 April 2008