Reduction of iron/zinc interactions using metal bound to the caseinophosphopeptide 1–25 of β-casein
Résumé
We used the isolated, perfused rat duodenal loop system to assess the influence of binding iron (Fe) to soluble 1–25 caseinophosphopeptide (β-CN (1–25)), produced by the hydrolysis of β casein, against the inhibition of its absorption by Zinc (Zn). Fe (100 μM) was perfused as Fe gluconate (Fe Gluc) or bound to the β-CN (1–25) (Fe CN), alone (controls) or in presence of Zn as Zn sulfate (Zn SO4) or as (Zn CN) at Fe:Zn ratios ranging from 2:1 to 1:5. Zn SO4 reduced significantly disappearance from the lumen (Q1) and net Fe absorption (FeAbs) at Fe:Zn ratios from 1:1.5 to 1:5 (p<0.001). Fe mucosal retention (Q2) did not change significantly. When Zn was provided as Zn CN, Q1, Q2 and Fe Abs did not significantly differ from control group for Fe Gluc. Zn SO4 and Zn CN did not reduce significantly Q1, Q2 nor FeAbs for Fe CN whatever ratios considered. Binding Fe to β-CN (1–25) prevented Zn from inhibiting its absorption by Zn and could have therapeutic applications in dietary supplementation of trace-elements.
Fichier principal
1-s2.0-S0271531799001219-main_{76768FBF-D7F9-460A-BAED-60ACCB444AE6}.pdf (631.57 Ko)
Télécharger le fichier
Origine : Accord explicite pour ce dépôt
Loading...