• OpenAccess
  • The calcium-binding activity of fish scale protein hydrolysates  [ASFE 2014]
  • DOI: 10.4236/jacen.2014.31B003   PP.11 - 15
  • Author(s)
  • Ruiyan Nie, Yuejiao Liu, Zunying Liu
  • 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.

  • Tilapia; Fish Scale; Calcium-Binding Activity; Peptide
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