Food fortification with iron with the intent of preventing anemia has represented a great challenge to the food industry. The mineral applied as a salt can induce lipid oxidation, sedimentation and sensory defects to the food in which it is added. Alternatively, minerals carried in complex or chelated forms present greater bioavailability and oxidative stability. Enzymatic hydrolysates produced from whey protein display certain peptides with physiologic actions and are called bioactive peptides. Amongst these actions, is the ability of binding to minerals and to carry them. Thus, the aim of this study was to obtain small molecular weight peptides from whey protein hydrolysis and to evaluate its ability of binding iron, optimize the complexation process and isolate and identify peptides with highest iron binding capacity. The best conditions of hydrolysis were selected through a rotational central composite design (RCDD) 22 for the Flavourzyme®, resulting in pH 6.7 and E/S 2.6%. Hydrolysates were fractionated by ultrafiltration system (cut-off 5 KDa) and characterized regarding its hydrophilic profile, total and free amino acids and the capacity of binding iron when considering its solubility in protein solutions. Syntheses of these complexes were optimized considering the solubility of iron in different proportion of peptides and pH values. Peptides with affinity for iron were separated and collected by resin IMAC-Fe III (FPLC), representing one third (1/3) of total mass of hydrolysate injected (33.7 mg). These peptides showed hydrophilic characteristics and elevated amino acid content such as histidine (62%) and proline (43%). Regarding optimization of the chelating process it was observed that the solubility of iron was higher when peptide to iron proportions were greater than (10:1) and pH greater than 4.0. Peptides smaller than 5 kDa showed high capacity to bind and stabilize iron under different medium conditions and therefore present high potential as food ingredient.