| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 5134166 | Food Chemistry | 2017 | 8 Pages |
â¢Structural folding and aggregation occurred during chelation process.â¢DPs enhanced Ca2+ uptake in presence of oxalate, phosphate, zinc in Caco-2 cells.â¢DPs promoted Ca uptake and counteracted the adverse effects of phytic acid in mice.â¢DPs regulated enterocyte proliferation and calbindinD9k mRNA expression.
The structure of the desalted duck egg white peptides-calcium chelate was characterized by fluorescence spectroscopy, fourier transform infrared spectroscopy, and dynamic light scattering. Characterization results showed structural folding and aggregation of amino acids or oligopeptides during the chelation process. Desalted duck egg white peptides enhanced the calcium uptake in the presence of oxalate, phosphate and zinc ions in Caco-2 monolayers. Animal model indicated that desalted duck egg white peptides effectively enhanced the mineral absorption and counteracted the deleterious effects of phytic acid. These findings suggested that desalted duck egg white peptides might promote calcium uptake in three pathways: 1) desalted duck egg white peptides bind with calcium to form soluble chelate and avoid precipitate; 2) the chelate is absorbed as small peptides by enterocyte; and 3) desalted duck egg white peptides regulate the proliferation and differentiation of enterocytes through the interaction with transient receptor potential vanilloid 6 calcium channel.
