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Sato, R., Shindo, M., Gunshin, H., Noguchi, T. and Naito, H. (1991) Characterization of phosphopeptide derived from bovine β-casein: An inhibitor to intra-intestinal pre-cipitation of calcium phosphate. Biochimica Biophysica Acta, 1077, 413-415. http://dx.doi.org/10.1016/0167-4838(91)90559-I

has been cited by the following article:

• TITLE: The calcium-binding activity of fish scale protein hydrolysates

  AUTHORS: Ruiyan Nie, Yuejiao Liu, Zunying Liu

  KEYWORDS: Tilapia; Fish Scale; Calcium-Binding Activity; Peptide

  JOURNAL NAME: Journal of Agricultural Chemistry and Environment, Vol.3 No.1B, January 16, 2014

  ABSTRACT: The calcium-binding activity of tilapia scale protein hydrolysates sequentially hydrolyzed by trypsin, flavor enzyme and pepsin were investigated. The hydrolysates were divided into four fractions using G-15 gel chromatography, and the F3 fraction has the higher calcium-binding activity of 196.3 mg/g. The UV-vis and the Fourier transform infrared spectroscopy (FTIR) demonstrate that the amino nitrogen atoms and the oxygen atoms belonging to the carboxylate groups are the primary binding sites for Ca2+. The X-ray diffraction and scanning electron microscopy (SEM) confirmed the reaction between the peptde and calcium. The results obtained indicated that this fish scale protein hydroly-sates have potential as functional foods for calcium-supplementation.