Exploration of iron-binding mode, digestion Kinetics, and iron absorption behavior of Antarctic Krill-derived heptapeptide-iron complex.

A novel heptapeptide LVDDHFL derived from Antarctic krill was used to assemble an iron complex, of which the iron-binding mode, in vitro digestion kinetics, and iron absorption behavior were explored. Fe2+ bound to one carboxyl oxygen atom of Asp at position 4 and the imidazole group of His at position 5 on the LVDDHFL peptide at a stoichiometric ratio of 1:2, which induced the folding of LVDDHFL to form a more orderly structure. LVDDHFL-iron significantly enhanced the solubility of iron as compared to FeSO4 in the gastroduodenal tract (P < 0.05), making it up to 80.92 ± 3.02% at the end of gastroduodenal digestion. Moreover, iron complexation can enhance the digestive stability of LVDDHFL with the peptide retention rate as 62.26 ± 2.60% and approximately 27.54% of LVDDHFL were degraded to hexapeptide LVDDHF. Nevertheless, the enhancement of LVDDHF - iron on iron absorption was comparable to that of LVDDHFL - iron, but better than that of FeSO4.