Novel calcium‐binding peptides from wheat protein hydrolysates: isolation, identification and mechanistic insights into calcium chelation

A novel pentapeptide (Lys-Glu-Gly-Val-Gln, KEGVQ) and hexapeptide (Asp-Lys-Val-Ile-Val-Pro, DKVIVP) were identified by LC-MS/MS. The calcium-binding capacity of them reached 110.37 and 114.59 mg g^-1, respectively. The KEGVQ-Ca and DKVIVP-Ca complexes formed new compounds with more compact and denser spherical structures. The carbonyl and carboxyl oxygen atoms of the Glu, Val and Gln residues contributed to the binding of calcium ions to KEGVQ. However, in the chelation of DKVIVP with Ca²⁺, Asp, Lys, Val and Pro residues showed considerable affinity. Moreover, electrostatic interactions were the main driving forces. These findings provide theoretical evidence for the chelation mechanism between KEGVQ, DKVIVP and Ca²⁺. This study not only puts forward a scientific basis for developing new calcium supplements from food resources, but also provides a feasible approach to isolate calcium-binding peptides and to clarify the chelation mechanism of calcium and peptides. © 2025 Society of Chemical Industry.