Improvement of zinc intestinal absorption and reduction of zinc/iron interaction using metal bound to the caseinophosphopeptide 1-25 of beta-casein.

@article{Peres1998ImprovementOZ,
  title={Improvement of zinc intestinal absorption and reduction of zinc/iron interaction using metal bound to the caseinophosphopeptide 1-25 of beta-casein.},
  author={Jean Michel Peres and Sa{\"i}d Bouhallab and Claire Petit and François Bureau and J L Maubois and Pierre Arhan and Dominique L Bougl{\'e}},
  journal={Reproduction, nutrition, development},
  year={1998},
  volume={38 4},
  pages={465-72}
}
Binding zinc (Zn) to soluble caseinophosphopeptides (CN), produced by the hydrolysis of caseins, improves its absorption and could prevent inhibition by other nutrients such as iron (Fe). The absorption of Zn (100 mumol/L) bound to the 1-25 CN (beta-CN(1-25)) of beta-casein, or as ZnSO4 was studied using the isolated, perfused rat intestinal loop system. Fe (Fe-CN or Fe gluconate (Fe Gluc)) was added at Zn/Fe ratios of 2:1, 1:5 and 1:10. Disappearance from the lumen (Q1) and net absorption… CONTINUE READING

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