Pubblicazione scientifica

Digestibility and IgE-Binding of Glycosylated Codfish Parvalbumin

FILONE TECNOLOGICO	TEMA
trasformazione e commercializzazione

RIASSUNTO

Food-processing conditions may alter the allergenicity of food proteins by different means. In this study, the effect of the glycosylation as a result of thermal treatment on the digestibility and IgE-binding of codfish parvalbumin is investigated. Native and glycosylated parvalbumins were digested with pepsin at various conditions relevant for the gastrointestinal tract. Intact proteins and peptides were analysed for apparent molecular weight and IgE-binding. Glycosylation did not substantially affect the digestion. Although the peptides resulting from digestion were relatively large (3 and 4 kDa), the IgE-binding was strongly diminished. However, the glycosylated parvalbumin had a strong propensity to form dimers and tetramers, and these multimers bound IgE intensely, suggesting stronger IgE-binding than monomeric parvalbumin. We conclude that glycosylation of codfish parvalbumin does not affect the digestibility of parvalbumin and that the peptides resulting from this digestion show low IgE-binding, regardless of glycosylation. Glycosylation of parvalbumin leads to the formation of higher order structures that are more potent IgE binders than native, monomeric parvalbumin. Therefore, food-processing conditions applied to fish allergen can potentially lead to increased allergenicity, even while the protein's digestibility is not affected by such processing.

DATA

Data di pubblicazione: 01/01/2013

AUTORI

DE JONGH HARMEN H J
ROBLES CARLOS LOPEZ
TIMMERMAN EEFJAN
NORDLEE JULIE A
LEE POI-WAH
BAUMERT JOSEPH L
HAMILTON ROBERT G
TAYLOR STEVE L
KOPPELMAN STEF J

ENTE DI AFFERENZA

TI FOOD & NUTRITION
FOOD PHYSICS GROUP DEPT AGROTECHNOLOGY & FOOD SCIENCE WAGENINGEN UNIV
FOOD ALLERGY RSCH & RESOURCE PROGRAM FOOD SCIENCE & TECH UNIV NEBRASKA LINCOLN 257 FOOD IND COMPLEX LINCOLN NE 68583 0919 USA
DEPT MEDICINE

RIVISTA

BioMed Research International, 2013, 756789

IMPACT FACTOR

2,140

indietro