Details

Autor(en) / Beteiligte

• Picariello, Gianluca
• Iacomino, Giuseppe
• Mamone, Gianfranco
• Ferranti, Pasquale
• Fierro, Olga
• Gianfrani, Carmen
• Di Luccia, Aldo
• Addeo, Francesco

Titel

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

Ist Teil von

• Food chemistry, 2013-08, Vol.139 (1-4), p.203-212

Ort / Verlag

Kidlington: Elsevier Ltd

Erscheinungsjahr

2013

Quelle

MEDLINE

Beschreibungen/Notizen

• ► 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.