Isolation of a novel calcium-binding peptide from phosvitin hydrolysates and the study of its calcium chelation mechanism. (March 2021) - Zhang, Xiaowei
Graphical abstract: Highlights: A novel calcium-binding peptide was identified and could bind 151.1 mg Ca/g peptide. The main binding sites were carboxyl oxygen atom and amino nitrogen atom. The bioavailability of this chelate was higher than CaCO3 and D-calcium gluconate. Abstract: A new peptide with strong calcium binding capacity was isolated from phosvitin hydrolysates. Taking calcium chelating rate as an indicator, phosvitin hydrolysates were separated gradually by anion-exchange chromatography, gel filtration chromatography and reversed-phase high performance liquid chromatography. A peptide with a molecular weight of 1106.44402 Da was identified by liquid chromatography-electrospray/mass spectrometry (LC-ESI/MS), and its amino acid sequence was DEEENDQVK, the calcium binding capacity reached 151.10 ± 3.57 mg/g. Its chelating mechanism was investigated. Results showed that, the β-sheet structure of peptide increased after adding calcium ion, and the main binding sites were carboxyl oxygen atom and amino nitrogen atom. In vitro simulated digestion experiments showed that, the solubility and dialysis rate of calcium in peptide-calcium chelate were higher than those in CaCO3 and D-calcium gluconate. This finding would promote the development of calcium supplements from food resources.