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Effects of molecular structure on the calcium-binding properties of phosphopeptides

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Abstract

Six synthetic phosphopeptides (SPP) and casein phosphopeptides (CPP) were obtained to investigate the relationship between the molecular structure of phosphopeptides and their calcium-binding property. SPP1, SPP2, SPP3, SPP4, SPP5, and SPP6 were synthesized with 0-3 continuous or discontinuous phosphorylated serines based on a core structure of casein phosphopeptides, respectively. CPP were acquired by pancreatin hydrolysis of casein and subsequent purification. The ranking of calcium-binding ability of the six synthetic phosphopeptides was SPP5 > SPP6 > SPP4 > SPP3 > SPP1 ~ SPP2. SPP4 was found to release calcium more easily in a simulated intestinal environment. CPP, contained various fragments ranged from 1 to 4 Ser(P)s, bound calcium slightly weaker than SPP6 that contained same amount of phosphorus with the CPP solution. The number and the position of phosphoserine residue are important factors for calcium-binding activities. SPP4, the phosphopeptide with two discontinuous phosphorylated serines, has the best calcium adsorption efficiency in a simulated intestinal environment among all the tested phosphopeptides.

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Acknowledgments

This work was supported by the Foundation for Sci & Tech Research Project of Zhejiang Province (2006C12096) and the National High Technology Research and Development Program of China (863 Program, 2008AA10Z313).

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Authors and Affiliations

  1. Department of Food Science and Nutrition, Zhejiang University, Huajiachi Campus, Hangzhou, China

    Hong Zong, Lijuan Peng, Saisai Zhang, Ying Lin & Fengqin Feng

  2. Department of Food Science and Nutrition, Zhejiang University, Zijingang Campus, Hangzhou, 310058, China

    Fengqin Feng

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  1. Hong Zong
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  2. Lijuan Peng
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Correspondence to Fengqin Feng.

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Zong, H., Peng, L., Zhang, S. et al. Effects of molecular structure on the calcium-binding properties of phosphopeptides. Eur Food Res Technol 235, 811–816 (2012). https://doi.org/10.1007/s00217-012-1809-5

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  • DOI: https://doi.org/10.1007/s00217-012-1809-5

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