The heat treatment and the gelation are strong determinants of the kinetics of milk proteins digestion and of the peripheral availability of amino acids |
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| Authors: | Florence Barbé Olivia Ménard Yann Le Gouar Caroline Buffière Marie-Hélène Famelart Béatrice Laroche Steven Le Feunteun Didier Dupont Didier Rémond |
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| Affiliation: | 1. INRA UMR 1253, Science et Technologie du Lait et de l’?uf, 65, rue de Saint Brieuc, 35000 Rennes, France;2. Agrocampus Ouest UMR 1253, Science et Technologie du Lait et de l’?uf, 35000 Rennes, France;3. Univ. Paris Sud-CNRS Supélec UMR 8506, Laboratoire des Signaux et Systèmes, 91192 Gif-sur-Yvette, France;4. INRA, UMR 1019, UNH, CRNH Auvergne, site de Theix, 63122 Saint-Genès Champanelle, 63000 Clermont-Ferrand, France;5. Clermont Université, Université d’Auvergne, Unité de Nutrition Humaine, BP 10448, 63000 Clermont-Ferrand, France;6. INRA UR 314, Mathématiques et Informatique Appliquées, 78352 Jouy-en-Josas, France;7. INRA UMR 0782, Génie et Microbiologie des Procédés Alimentaires, 78850 Thiverval-Grignon, France;8. AgroParisTech UMR 0782, Génie et Microbiologie des Procédés Alimentaires, 78850 Thiverval-Grignon, France;1. Institute of Agri-Food and Land Use, School of Biological Sciences, Queen''s University Belfast, Belfast, Northern Ireland, UK;2. Institute of Agri-Food and Land Use, ASSET centre, Queen''s University Belfast, Belfast, Northern Ireland, UK |
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| Abstract: | This study aimed to determine the kinetics of milk protein digestion and amino acid absorption after ingestion of four dairy matrices by six minipigs: unheated or heated skim milk and corresponding rennet gels. Digestive contents and plasma samples were collected over a 7 h-period after meal ingestion. Gelation of milk slowed down the outflow of the meal from the stomach and the subsequent absorption of amino acids, and decreased their bioavailability in peripheral blood. The gelled rennet matrices also led to low levels of milk proteins at the duodenum. Caseins and β-lactoglobulin, respectively, were sensitive and resistant to hydrolysis in the stomach with the unheated matrices, but showed similar digestion with the heated matrices, with a heat-induced susceptibility to hydrolysis for β-lactoglobulin. These results suggest a significant influence of the meal microstructure (resulting from heat treatment) and macrostructure (resulting from gelation process) on the different steps of milk proteins digestion. |
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