Purification of an iron‐binding peptide from scad (Decapterus maruadsi) processing by‐products and its effects on iron absorption by Caco‐2 cells.

This work was aimed at producing peptides containing iron‐binding capabilities from scad (Decapterus maruadsi) processing by‐product with alcalase hydrolysis. The chelating peptides were purified by ultrafiltration, immobilized‐metal affinity chromatography, gel filtration chromatography, and reversed‐phase high‐performance liquid chromatography. A novel iron‐binding peptide was purified with 1,386.63 Da molecular weight and amino acid sequence of QKGTYDDYVEGL. The peptide binds to iron mainly through carboxyl and hydroxyl oxygen bonds. The iron‐binding peptide can significantly promote the absorption of inorganic iron in Caco‐2 cells. These results have contributed to development of the peptide from scad processing by‐products hydrolyzate in iron supplementations. Practical applications: Iron deficiency is one of the most common and widespread nutritional disorders in the world. Iron‐peptide chelates may be suitable for iron‐fortification. Our study shows that a peptide purified from scad processing by‐product has iron‐chelating activity, and significantly increases iron absorption by Caco‐2 cells. Hence, this peptide has potential application as a novel carrier for enhancing iron absorption. [ABSTRACT FROM AUTHOR]