Heating and glycation of [i]β-lactoglobulin[/i] and[i] β-casein[/i]: Aggregation and[i] in vitro[/i] digestion - Archive ouverte HAL Accéder directement au contenu
Article Dans Une Revue Food Research International Année : 2014

Heating and glycation of [i]β-lactoglobulin[/i] and[i] β-casein[/i]: Aggregation and[i] in vitro[/i] digestion

Résumé

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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Dates et versions

hal-01205074 , version 1 (24-09-2015)

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Michèle da Silva Pinto, Joelle Léonil, Gwenaele Henry, Chantal Cauty, Antonio F. Carvalho, et al.. Heating and glycation of [i]β-lactoglobulin[/i] and[i] β-casein[/i]: Aggregation and[i] in vitro[/i] digestion. Food Research International, 2014, 55, pp.70-76. ⟨10.1016/j.foodres.2013.10.030⟩. ⟨hal-01205074⟩
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