The calcium-binding activity of fish scale protein hydrolysates

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 hydrolysates have potential as functional foods for calcium-supplementation.