Structural Characteristics and Stability of Corn Peptide-iron Chelates
Article
Figures
Metrics
Preview PDF
Reference
Related
Cited by
Materials
Abstract:
Corn peptide-iron chelates serve a dual purpose, enhancing the utilization of corn peptides while also offering a novel approach for the development of iron supplements. To examine the structural properties and thermal stability of corn peptide-iron chelates, samples of this compound were prepared from corn peptides and ferrous chloride. Following ultraviolet spectroscopy and thermogravimetric analysis, the binding sites of the identified corn peptide fragments and ferrous ions were simulated by molecular docking. The stability of the corn peptide–iron chelate was observed at different temperatures and pH values, as well as under different in vitro digestion conditions. The results showed that the ultraviolet absorption peak changed. More specifically, the characteristic absorption peak shifted from 274.99 nm to 275.01 nm. Moreover, the corn peptide and corn peptide-iron chelate were compared and found to differ in a number of their pro perties. Thermogravimetric analysis revealed residual rates of 34.94% and 18.74% for corn chelate and peptide, respectively, while thermal stability of the corn peptide-iron chelate was found to be significantly higher that of the corn peptide. The binding energy levels of FSAASYPDLIDALP and LQQRQQLLNPL with Fe2+ were ‒50.50 and ‒48.61 kJ/mol, respectively, and the amino group of Asp8 (aspartic acid) was found to provide the ligand site. In addition, Pro7 (proline), Ser5 (serine), Tyr6 (tyrosine), and Leu7 (leucine) were found to bind to the ferrous ions to form hydrophobic interactions. The relative molecular masses were mostly below 1 000 u under the action of different temperatures. In addition, small peptides were more easily chelated and absorbed, and were stable under relatively alkaline conditions.
