Iron Tissue Storage and Hemoglobin Levels of Deficient Rats Repleted with Iron Bound to the Caseinophosphopeptide 1−25 of β-Casein

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Abstract
Caseinophosphopeptides (CPP) issued from enzyme digestion of caseins bind cations and keep them soluble in the digestive tract. They could be used as ligands to improve iron (Fe) bioavailability. Fe-deficient young rats were repleted with Fe (40 or 200 mg/kg of diet) bound either to the β-CN (1−25) of β-casein or to whole β-casein or as FeSO4. A control pair-fed group was given 200 mg of Fe (FeSO4)/kg of diet for 6 weeks. After repletion, hemoglobin concentration of the control group was reached only by the β-CN (1−25) animals fed 200 mg of Fe/kg; β-CN (1−25) bound Fe (40 and 200 mg) produced higher Fe liver and spleen stores than FeSO4. Binding Fe to the whole, nonhydrolyzed β-casein gave results intermediate between the other experimental groups. Binding Fe to phosphoserine residues of low molecular weight CPP improved its ability to cure anemia and to restore iron tissue stores, as compared to Fe bound to the whole casein and to inorganic salts. Keywords: Iron; bioavailability; tissue storage; hemoglobin; casein phosphopeptide; milk proteins; rat