Journal
FOOD CHEMISTRY
Volume 240, Issue -, Pages 1227-1232Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.foodchem.2017.08.063
Keywords
Whey peptides; Zinc; Gastric stability; Bioaccessibility; Surface charge
Funding
- Natural Sciences and Engineering Research Council of Canada (NSERC) [RGPIN 435865-2013]
- Canada Foundation for Innovation (CFI)
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Gastrointestinal stability of zinc-peptide complexes is essential for zinc delivery. As peptide surface charge can influence their metal complex stability, we evaluated the zinc-chelating capacity and stability of zinc complexes of whey protein hydrolysates (WPH), produced with Everlase (WPH-Ever; xi-potential, -39 mV) and papain (WPH-Pap; xi-potential, -7 mV), during simulated digestion. WPH-Ever had lower amount of zinc-binding amino acids but showed higher zinc-chelating capacity than WPH-Pap. This is attributable to the highly anionic surface charge of WPH-Ever for electrostatic interaction with zinc. Release of zinc during peptic digestion was lower for WPH-Ever-zinc, and over 50% of zinc remained bound in both peptide complexes after peptic-pancreatic digestion. Fourier transform infrared spectroscopy suggests the involvement of carboxylate ion, and sidechain carbon-oxygen of aspartate/glutamate and serine/threonine in zinc-peptide complexation. The findings indicate that strong zinc chelation can promote gastric stability and impede intestinal release, for peptides intended for use as dietary zinc carriers.
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