Identification, characterization and binding sites prediction of calcium transporter-embryo egg-derived egg white peptides.

In order to provide an efficient calcium transporter for the development of calcium supplement products, embryo eggs were selected for incubation. Carrying out calcium ions chelation on the embryo egg-derived egg white peptides (EED-EWPs) with high calcium binding activity produced incubation. The changes of EED-EWPs before and after chelation with calcium ions were compared, ζ-potential absolute value increased significantly, indicating that the embryo egg-derived egg white peptides calcium chelates (EED-EWPs-Ca) was successfully formed. Calcium binding activity results displayed that EED-EWPs on the 9th day of incubation had the highest calcium binding ability (6.96 μg/mg), which was 1.17 times that before incubation (5.97 μg/mg). EED-EWPs were isolated by IMAC metal chelating preloaded column, calcium binding amount was improved to 17.88 μg/mg, which was about 3 times that of those before isolation. The EED-EWPs were analyzed by mass spectrometry, six peptides with high calcium binding ability were identified. The mechanism of promoting calcium absorption of EED-EWPs produced during incubation was investigated by molecular docking with TRPV6 (a key protein for calcium transporter in the human small intestine). Results elucidated that amino and carboxyl groups in EED-EWPs were possible sites for calcium ions binding. This study would provide an efficient calcium transporter with high nutritional value for the development of calcium supplement products. [ABSTRACT FROM AUTHOR]