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.