Abstract:The purpose of this paper was to prepare collagen peptides with calcium-chelating ability from tilapia fish bone. Bone collagen was used as experimental material after pre-meat including removing meat from the skeleton and decalcification. With calcium chelation activity as the index, papain was selected as the acting enzyme. The single factor and orthogonal test were employed to optimize the enzymolysis process of preparation of tilapia bone collagen. The Tilapia calcium chelating peptide, obtained by enzymatic hydrolysis under optimal conditions, was used as the target for the determination of their molecular weight and amino acid composition. The results showed that the optimum enzymolysis process conditions were as follows: Enzymolysis time (4.5 h), pH (6.5), enzymolysis temperature (62 ℃), enzyme to substrate ratio (0.6%). Tilapia bone collagen calcium chelating peptide was a kind of function substance composed of small molecular peptides; By comparing the amino acid composition of tilapia bone collagen calcium chelating peptide and its calcium-peptide chelated, it is found that amino acids such as cystine, aspartic acid, serine, glutamic acid, glycine, histidine and lysine played an important role in the calcium chelating capacity of the active peptide.
