| Literature DB >> 27765248 |
Tao Hou1, Weiwei Liu1, Wen Shi1, Zhili Ma1, Hui He2.
Abstract
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.Entities:
Keywords: Caco-2 monolayer model; Calcium bioavailability; Calcium chloride (PubChem CID: 5284359); Desalted duck egg white peptides; Phytic acid; Phytic acid (PubChem CID: 890); Potassium bromide (PubChem CID: 253877); Sodium oxalate (PubChem CID: 6125); Sodium tripolyphosphate (PubChem CID: 24455); Transient receptor potential vanilloid 6
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Year: 2016 PMID： 27765248 DOI： 10.1016/j.foodchem.2016.09.166
Source DB: PubMed Journal: Food Chem ISSN： 0308-8146 Impact factor: 7.514