Transport across Caco-2 monolayers of peptides arising from in vitro digestion of bovine milk proteins.
Food Chem
; 139(1-4): 203-12, 2013 Aug 15.
Article
em En
| MEDLINE
| ID: mdl-23561097
ABSTRACT
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 ß-CN were detected. The absorption behaviour of two resistant ß-lactoglobulin (ß-Lg) domains, ß-Lg 125-135 and ß-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 ß-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.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Peptídeos
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Caseínas
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Membrana Celular
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Digestão
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Proteínas do Leite
Idioma:
En
Ano de publicação:
2013
Tipo de documento:
Article