Heating and glycation of [i]β-lactoglobulin[/i] and[i] β-casein[/i]: Aggregation and[i] in vitro[/i] digestion
2014
da Silva Pinto, Michèle | Léonil, Joelle | Henry, Gwenaele | Cauty, Chantal | Carvalho, Antonio F. | Bouhallab, Said | Science et Technologie du Lait et de l'Oeuf (STLO) ; Institut National de la Recherche Agronomique (INRA)-AGROCAMPUS OUEST | Laboratoire de Physiologie et Génomique des Poissons (LPGP) ; Institut National de la Recherche Agronomique (INRA)-Structure Fédérative de Recherche en Biologie et Santé de Rennes (Biosit : Biologie - Santé - Innovation Technologique) | Laboratory of Research in Milk Products ; Universidade Federal de Viçosa [Brasil] = Federal University of Viçosa [Brazil] = Université fédérale de Viçosa [Brésil] (UFV [Brésil]) | Capes (Coordenação de Aperfeiçoamento de Pessoal de Nível Superior, Brazil), CNPq (Conselho Nacional de Desenvolvimento Cientifico e Tecnológico, Brazil), Fapemig (Fundação de Amparo à Pesquisa, Brazil), INRA
Heat treatment is commonly used in dairy technology. Usually, milk is heated and cooled many times before to obtain the final product and milk components are then subject to cumulative heat treatments. In the present work, we investigated the heat induced aggregation (90 °C until 24 h) of two model proteins, β-lactoglobulin (β-Lg) and β-casein (β-CN), in the presence of glucose and subsequent consequences on simulated gastroduodenal digestion. Protein aggregation and digestionwere monitored using polyacrylamide gel electrophoresis, size exclusion chromatography, dynamic light scattering and transmission electron microscopy. Concomitant heating and protein glycation affect aggregation kinetics as well as protein sensitivity to enzymatic digestion. Spherical covalently linked aggregates were favored in the case of β-CN in the presence of glucose. Glucose limited the formation of twisted fibrils fromβ-Lg. We clearly showed that aggregates of both proteins formed in the presence of glucose were more resistant to enzymatic digestion. Those formed from β-Lg being highly resistant and still present at the end of simulated gastro-duodenal process. These findings underline the importance not only of the aggregation as such but also of the nature of formed aggregates on protein digestibility.
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