Preparation Of Tilapia Bone Collagen Calcium Chelating Peptide By Enzymatic Hydrolysis
Keywords
Tilapia Bone Enzymolysis Calcium Chelating Peptide Calcium-Peptide Chelating Molecular Weight Distribution Amino Acid Compositiontilapia Bone Enzymolysis Calcium Chelating Peptide Molecular Weight Distribution Amino Acid Composition
Abstract
In this study, tilapia bone collagen was used as raw material to prepare active peptides with good calcium chelating ability through enzymatic hydrolysis. Using calcium chelating activity as an indicator, the tilapia bone collagen obtained from the tilapia skeleton after pre-treatment such as meat removal and decalcification was enzymatically hydrolyzed by papain to prepare tilapia bone collagen peptide. Cross-experiment was conducted to optimize the enzymatic hydrolysis process for preparing tilapia collagen chelated peptide. At the same time, the molecular weight and amino acid composition of tilapia bone collagen calcium chelate peptide obtained by enzymatic hydrolysis under optimal conditions were analyzed. The results showed that the optimal enzymatic hydrolysis process conditions were: enzymatic hydrolysis time 4.5 h, pH 6.5, enzymatic hydrolysis temperature 62 ¡ãC, and enzyme bottom ratio 0.6%. Tilapia bone collagen calcium chelating peptide is a type of small molecule functionally active peptide. At the same time, by comparing the amino acid composition of tilapia bone collagen calcium chelate peptide and its calcium-peptide chelate, it was found that cystine, aspartic acid, serine, glutamic acid, glycine, histidine and lysine and other amino acids Plays an important role in the calcium chelating ability of active peptides. 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, papin 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 ¡æ), 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.
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Original research was done by Liao Wanwen
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