Isolation, identification, and chelation mechanism of ferrous-chelating peptide from peanut protein hydrolysate.

Background: Peanut peptides can chelate iron but their chelation mechanism remains unclear. The purpose of this study is to separate peanut ferrous-chelating peptides and explore the chelation mechanism of peanut peptides with iron.

Results: Peanut peptide component F-122, which had a higher chelation rate, was separated using ultrafiltration, gel filtration chromatography, and ion exchange chromatography, achieving a ferrous chelation rate of 90.7%. Six peptide segments were screened and their amino acid sequences were identified by liquid chromatography-tandem mass spectrometry (LC-MS/MS). Spectral analysis confirmed that the chelation between peanut peptides and ferrous ions occurred and a new substance was formed. Molecular docking simulation indicated that the amino acids in peanut peptides involved in the chelating reaction were glutamic acid, arginine, glycine, threonine, phenylalanine, and lysine. The binding sites included the main chain oxygen atom, side chain oxygen atom, and carboxyl oxygen atom of amino acid.

Conclusion: The isolated peanut peptide had a higher ferrous-chelation rate. The chelating mechanism of peanut peptide with ferrous ion was elucidated. This study provides a theoretical basis for the development of new peptide-ferrous preparations. © 2024 Society of Chemical Industry.