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  • a Tianjin University of Science and Technology, Tianjin 300457, People's Republic of China
  • | b Tianjin University, Tianjin 300072, People's Republic of China
  • | c Collaborative Innovation Center of Chemical Science and Engineering (Tianjin), Tianjin 300072, People's Republic of China
  • | d Tianjin Key Laboratory of Membrane Science and Desalination Technology, Tianjin 300072, People's Republic of China
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Casein peptides with calcium-chelating capacity were rapidly enriched by using a novel ceramic matrix (CM)-based Ti4+-IMAC adsorbent. The ability of calcium-chelating peptides (CCPs) to bind calcium and the physical properties of complexes formed between CCPs and calcium were investigated. Results demonstrated that the amount of calcium bound depended on the degree of hydrolysis (DH) of casein hydrolysates. The highest calcium binding capacity (683 mg g−1) occurred when bovine casein was hydrolysed by pancreatin at a DH of 0.14%, meanwhile, the calcium content of CCPs-Ca complex exhibited the maximum level (134.96 mg g−1). In addition, CCPs showed a higher radical scavenging capacity (50 µg ml−1; 99% inhibition, or an equivalent activity of 9.91×10−3 M Trolox) compared to casein digest. Moreover, Fourier-transform infrared spectroscopy and fluorescence spectroscopy were used to explore the interaction between CPPs and calcium, and the results demonstrated that phosphoserine residues as well as COO- groups of CCPs were involved in the formation of CCPs-Ca complex.

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