Isolation and identification of calcium-chelating peptides from Pacific cod skin gelatin and their binding properties with calcium

Food & Function
Wenfei WuXue Zhao

Abstract

A calcium-chelating peptide is considered to have the ability to improve calcium absorption. In this study, Pacific cod skin gelatin hydrolysates treated with trypsin for 120 min exhibited higher calcium-chelating activity. Sequential chromatography, involving hydroxyapatite affinity chromatography and reversed phase high performance liquid chromatography, was used for the purification of calcium-chelating peptides. Two novel peptides with the typical characteristics of collagen were sequenced as GDKGESGEAGER and GEKGEGGHR based on LC-HRMS/MS, which showed a high affinity to calcium. Calcium-peptide complexation was further characterized by ESI-MS (MS and MS/MS) and FTIR spectroscopy. The results showed that the complexation of the two peptides with calcium was conducted mainly at the ratio of 1 : 1. The amino terminal group and the peptide bond of the peptide backbone as well as the amino group of the lysine side chain and the carboxylate of the glutamate side chain were the possible calcium binding sites for the two peptides. Meanwhile, several amino acid side chain groups, including the hydroxyl (Ser) and carboxylate (Asp) of GDKGESGEAGER and the imine (His) of GEKGEGGHR, were crucial in the complexation. The arginine residu...Continue Reading

References

Sep 18, 2003·Journal of Agricultural and Food Chemistry·Wichittra DaengprokYoshinori Mine
Aug 10, 2007·Acta Biochimica Et Biophysica Sinica·Jilie Kong, Shaoning Yu
Oct 22, 2016·Food Chemistry·Zhi-Hong ZhangMan-Sheng Wang

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Citations

May 20, 2020·Molecules : a Journal of Synthetic Chemistry and Natural Product Chemistry·Jianing WangYanchuan Guo
Dec 29, 2020·Journal of Agricultural and Food Chemistry·Suyin ZhuYang Yuan

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Methods Mentioned

BETA
flame atomic absorption spectroscopy

Software Mentioned

OMNIC
Protein Pilot
SPSS

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