Complexing iron with organic compounds has been considered an alternative strategy to mitigate the problems associated with the level of bioavailable iron and the acceptability of products supplemented with this mineral. CMP contains specific amino acids associated with iron binding. The present study aims to optimize the conditions of Fe/CMP complex formation and understand the molecular basis of interactions between CMP and iron ions. Results showed that CMP can bind ferrous iron in a 1:1.5 M ratio, forming a stable peptide-iron complex, where CMP assembles in a tetrameric form. FTIR spectra indicated that iron binding altered the secondary structures of CMP. The iron-binding sites of CMP corresponded primarily to acid residues of Glu, Asp and sialic acid. Moreover, Fe/CMP complex remained stable in a wide pH range (2.0-6.5), suggesting the adequacy to be efficiently added in food or beverages and to keeping complexed in the digestion environment. Finally, Fe/CMP complex was added to a commercial beverage (2 mg of Fe per serving of beverage) and no changes were observed in their colour during storage. A model to explain the binding between CMP and iron is proposed. These results suggest a potential application of this peptide for iron fortification.
Keywords: Beverage; Caseinglycomacropeptide; Complexes stability; Interaction; Iron fortification; Particle size.
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