Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
6396088 | Food Research International | 2015 | 7 Pages |
Abstract
Binding and solubilization of ferric iron by food peptides, released during digestion, facilitate intestinal iron absorption. In the present study, we investigated the release of iron-binding peptides during in vitro gastrointestinal digestion of chicken (Gallus gallus) egg white. The iron-binding activity of the egg white protein increased upon gastrointestinal digestion. The iron-binding fraction of egg white digesta was purified by gel filtration chromatography followed by reverse phase HPLC. Subsequently, this fraction was identified as an internal fragment of ovalbumin (DKLPGFGDS(PO4)IEAQ, 61-73 residues, GenBank AAB59956.1) by MALDI-MS/MS followed by de novo sequencing. The synthetic peptide corresponding to the identified iron-binding peptide sequence bound and increased the 59Fe-iron uptake. Further, the synthetic peptide also stimulated the iron-induced ferritin synthesis in intestinal Caco-2 cells. While, dephosphorylation of synthetic peptide completely inhibited the iron-binding activity, methyl-esterification of its carboxyl groups partially inhibited the activity. These results suggest that food derived peptides modulate intestinal iron absorption and that the isolated iron-binding egg peptide could be a potential nutraceutical for improving iron absorption.
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Food Science
Authors
Ravindranadh Palika, Purna Chandra Mashurabad, Madhavan K. Nair, G. Bhanuprakash Reddy, Raghu Pullakhandam,