JACEN  Vol.3 No.1 B , January 2014
The calcium-binding activity of fish scale protein hydrolysates

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.

Cite this paper: R. Nie, Y. Liu and Z. Liu, "The calcium-binding activity of fish scale protein hydrolysates," Journal of Agricultural Chemistry and Environment, Vol. 3 No. 1, 2014, pp. 11-15. doi: 10.4236/jacen.2014.31B003.

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