罗非鱼骨胶原钙螯合肽的酶解制备

Preparation of Tilapia Bone Collagen Calcium Chelating Peptides by Enzymatic Hydrolysis

摘要:

本研究以罗非鱼骨胶原蛋白为原料酶解制备具有良好钙螯能力性的活性肽。以钙螯合活性为指标，将罗非鱼骨架经过脱肉、脱钙等前处理获得的罗非鱼骨胶原蛋白通过木瓜蛋白酶酶解制备得到罗非鱼骨胶原蛋白肽，通过单因素及正交试验对制备罗非鱼骨胶原螯合肽的酶解工艺进行优化。同时对最优条件下酶解获得的罗非鱼骨胶原钙螯合肽的分子量及氨基酸组成进行分析。结果表明，最优酶解工艺条件为：酶解时间4.5 h，pH 6.5，酶解温度62 ℃，酶底比0.6%。罗非鱼骨胶原钙螯合肽是一类小分子功能活性肽。同时通过对比罗非鱼骨胶原钙螯合肽及其钙-肽螯合物氨基酸组成，发现胱氨酸、天冬氨酸、丝氨酸、谷氨酸、甘氨酸、组氨酸和赖氨酸等氨基酸对活性肽的钙螯合能力起到重要作用。

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.