Calcium binding to herring egg phosphopeptides: Binding characteristics, conformational structure and intermolecular forces. (25th April 2020)

• Record Type: Journal Article
• Authors: Sun, Na; Wang, Yixing; Bao, Zhijie; Cui, Pengbo; Wang, Shan; Lin, Songyi
• Is Part Of: Food chemistry. Volume 310(2020)
• Publication Date: 2020-04-25
• Subjects: Herring egg -- Phosphopeptides -- Calcium binding -- Conformational structure -- Nanoparticle -- Intermolecular force; Food -- Analysis -- Periodicals; Food -- Composition -- Periodicals; 664
• DOI: 10.1016/j.foodchem.2019.125867
• Languages: English
• ISSNs: 0308-8146

Abstract

Highlights: Phosphorylation could increase the calcium-binding ability of herring egg peptides. Asp, Glu and Ser were responsible for calcium-chelating capacity of HEPPs. The calcium-binding sites of HEPPs involved carboxyl, carbonyl and phosphate groups. Calcium induced structural folding of HEPPs, thus assembling into nanoparticles. The HEPPs-Ca nanoparticles were stabilized by non-covalent bond forces. Abstract: Phosphorylation could improve functional characteristics of proteins/peptides, and might be used in the functional improvement of herring egg peptides owing to their enriched phosphorylation sites. The present study aimed to study the effect of phosphorylation on calcium-binding ability of herring egg peptides, and investigate the conformational structure and intermolecular forces of herring egg phosphopeptides (HEPPs)-calcium complex. The HEPPs were found to be superior in calcium-binding activities, as compared to the non-phosphorylated variant. This finding might be attributed to the interaction between calcium ions and the introduced phosphate groups of HEPPs. Calcium favored the formation of β-sheet structure on the HEPPs and induced structural folding, thus assembling into spherical nanoparticles. The conformation of HEPPs-Ca nanoparticles was formed and stabilized mainly by hydrophobic interaction, hydrogen bonds and electrostatic interaction.