Fractional purification process and activity analysis of wheat calcium ion chelating peptides
Year: 2025
Type: article
Abstract: Calcium chelate peptide is a new type of calcium supplement with good absorption properties, bioavailability, safety and stability. This study has prepared calcium chelated peptide from gluten, and obtained peptide sequences with high activity, while analyzing their digestive characteristics and stability. The enzymatic hydrolysis process conditions was optimized using response surface methodology. And the optimal conditions for enzymatic hydrolysis were temperature 55°C, pH 8.5, and an enzyme ratio of 2.63:1 (alkaline protease to flavor protease), with liquid-to-solid ratio set at 20:1. The calcium chelation rate for gluten hydrolysate was 40.1%. Following fractional purification, peptides with a molecular weight below 500Da exhibited the highest chelating activity (51.1%). LC-MS/MS analysis identified 1224 distinct peptide sequences, among which V.YIPPY.C (WCP1) exhibited a higher calcium chelation rate after selection and molecular docking studies. The synthesized WCP1 displayed a calcium chelation rate of 53.5%. FTIR confirmed that both carboxyl and phosphate groups play crucial roles in mediating interactions between calcium ions and wheat polypeptides. CD revealed that the structure became more compact postchelation. Furthermore, stability experiments indicated that the calcium chelate peptides displayed notable resistance to digestion along with pH stability and thermal stability. This study can provide technical support for gluten flour deep processing and functional product development.
Authors: Lai Wei, Fang Wang, Jiahui Tan, Xiyi Chen, Ziyan Zhang, Jie Sun
Institution: Qingdao University
Language: English
Subfield: Molecular Biology
Domain: Life Sciences
SDG: Zero hunger
Open Access status: diamond
OpenAlex ID: W4413304747