| Literature DB >> 27719884 |
Abstract
The transepithelial transport routes of casein-derived peptides with different molecular weights (MWs) were investigated using a Caco-2 cell monolayer. The peptidase hydrolysis during transport was also studied. The results indicate that the paracellular route was the main pathway for F1 (1600-1300Da) and F2 (1000-500Da), and the bioavailabilities were 10.66% and 9.54%, respectively. Peptidase hydrolysis results reveal that brush-border peptidases (BBPs) as well as some other peptidases were responsible for peptide degradation in the paracellular route. The maximum hydrolysis rate of the former was 6.91 and 5.59μM Gly/min for the latter. However, PepT1 was involved in the transport of F3 (<500Da) and its bioavailability was 16.23%. BBPs were the main peptidases involved in the PepT1 transport and the maximum hydrolysis rate was 11.4μM Gly/min. Furthermore, we found that the amino acid sequence of di- and tripeptides might affect their bioavailabilities significantly.Entities:
Keywords: Bioavailability; Brush-border peptidase (BBP); Casein peptide; Hydrolysis; Molecular weight (MW); Transepithelial transport
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Year: 2016 PMID: 27719884 DOI: 10.1016/j.foodchem.2016.08.106
Source DB: PubMed Journal: Food Chem ISSN: 0308-8146 Impact factor: 7.514