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Título

Hydrolysis under high hydrostatic pressure as a means to reduce the binding of β-lactoglobulin to immunoglobulin E from human sera

AutorChicón, Rosa; Belloque, Josefina ; Alonso, Elena; Martín-Álvarez, Pedro J. ; López-Fandiño, Rosina
Fecha de publicaciónjul-2008
EditorInternational Association for Food Protection
CitaciónJournal of Food Protection 71(7): 1453-1459 (2008)
ResumenCows' milk allergy is the most frequent food allergy in children, and β-lactoglobulin (β-Lg) is a major allergen. Milk-based hypoallergenic ingredients are manufactured by enzymatic hydrolysis, a process that could be improved by the application of high-pressure treatments. This study showed that the treatment of β-Lg dissolved in buffer with chymotrypsin and trypsin under high pressure for relatively short times accelerated proteolysis by leading to a rapid removal of the intact protein. The rapid proteolysis of the β-Lg substrate under pressure led to the production, in 20 min, of hydrolysates with lower immunoglobulin (Ig) G binding than those produced in 8 h (chymotrypsin) or 48 h (trypsin) at atmospheric pressure. However, those hydrolysates retained some residual IgE-binding properties that could be traced to the preferential release, during the initial stages of proteolysis, of peptides containing IgE epitopes, such as (Val-41-Lys-60), (Leu-149-Ile-162), and (Ser-21-Arg-40). The formation of these fragments was favored when proteolysis was conducted under high pressure due to the preferential hydrolysis of Arg-40 and Arg-148 by trypsin, and Tyr-42 and Leu-149 by chymotrypsin, all located at the dimer interface of β-Lg or very close to it. Although our results do not support that trypsin and chymotrypsin under high pressure selectively address the allergenic regions of β-Lg, it is possible to select the conditions that quickly produce hydrolysates with reduced potential allergenicity that could be used in hypoallergenic foods.
Descripción7 pages.-- PMID: 18680946 [PubMed].
Versión del editorhttp://www.ingentaconnect.com/content/iafp/jfp/2008/00000071/00000007/art00019
URIhttp://hdl.handle.net/10261/10395
ISSN0362-028X
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