Transport across Caco-2 monolayers of peptides arising from in vitro digestion of bovine milk proteins

► Casein and whey proteins were in vitro digested and applied to Caco-2 monolayers. ► Resistant peptides able to translocate across monolayers were characterised. ► Minor amount of supposed bioactive peptides were detected. ► After digestion milk proteins almost completely lost the IgE-binging prope...

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Published in:Food chemistry Vol. 139; no. 1-4; pp. 203 - 212
Main Authors: Picariello, Gianluca, Iacomino, Giuseppe, Mamone, Gianfranco, Ferranti, Pasquale, Fierro, Olga, Gianfrani, Carmen, Di Luccia, Aldo, Addeo, Francesco
Format: Journal Article
Language:English
Published: Kidlington Elsevier Ltd 15-08-2013
Elsevier
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Summary:► Casein and whey proteins were in vitro digested and applied to Caco-2 monolayers. ► Resistant peptides able to translocate across monolayers were characterised. ► Minor amount of supposed bioactive peptides were detected. ► After digestion milk proteins almost completely lost the IgE-binging properties. ► β-Lg 127–135 is a possible “immune sensitising factors” in vivo. The entire panel of peptides produced from caseins (CN) and whey proteins (WP) that survive in vitro sequential gastro-pancreatic digestion and translocate across monolayers of Caco-2 cells, used as a model of the intestinal epithelium, has been characterised by HPLC and mass spectrometry. Among the milk-derived bioactive peptides, only minor amounts of mono-phosphorylated peptides arising from αs1- and β-CN were detected. The absorption behaviour of two resistant β-lactoglobulin (β-Lg) domains, β-Lg 125–135 and β-Lg 40–60, was studied in detail using synthetic peptides. The IgE-binding properties of the digests recovered from the apical and basolateral monolayer compartments were evaluated by dot-blot, using the sera of milk allergic children (N=5). Outcomes indicated β-Lg 127–135 as a possible “immune sensitising factor” in vivo. The almost complete loss of the IgE-affinity of CN and WP after digestion points out the need to design in vivo experiments to track the metabolic fate of dietary proteins.
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ISSN:0308-8146
1873-7072
DOI:10.1016/j.foodchem.2013.01.063