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当前位置: 首页 > 文章 > 白鲢鱼骨胶原多肽螯合钙的工艺优化 食品科学 2014,35 (10) 76-81
Position: Home > Articles > Optimization of the Preparation of Calcium-Chelating Polypeptides from Silver Carp Bone Collagen FOOD SCIENCE 2014,35 (10) 76-81

白鲢鱼骨胶原多肽螯合钙的工艺优化

作  者：
刘闪;刘良忠;李小娜;刘亮;王燕
单  位：
武汉轻工大学食品科学与工程学院,武汉市水产品加工工程技术研究中心
关键词：
鱼骨;胶原多肽;螯合钙
摘  要：
为减少淡水鱼加工过程中副产物对环境的污染和资源的浪费、提高淡水鱼的附加值,对白鲢鱼骨制备胶原多肽螯合钙的工艺进行研究。以白鲢鱼骨和氯化钙为原料,在一定条件下制备胶原多肽螯合钙,考察温度、鱼骨胶原多肽与氯化钙的质量比、时间、pH值对螯合率和螯合物中钙含量的影响。根据单因素试验结果,对胶原多肽螯合钙工艺进行四因子二次正交旋转设计优化,得到鱼骨胶原多肽螯合钙的最佳工艺参数为温度42℃、时间38 min、鱼骨胶原多肽与氯化钙的质量比2.1∶1、pH 6.8,此条件下的螯合率和螯合物中的钙含量分别为80.4%和12.1%。对螯合钙进行氨基酸组成成分分析,其总氨基酸含量为61.03%,且具备典型的胶原蛋白氨基酸组成特征。红外光谱扫描和电镜扫描观察表明:钙离子与胶原多肽发生了螯合反应,结合方式有离子结合、配位结合和吸附作用。
译  名：
Optimization of the Preparation of Calcium-Chelating Polypeptides from Silver Carp Bone Collagen
作  者：
LIU Shan;LIU Liang-zhong;LI Xiao-na;LIU Liang;WANG Yan;Aquatic Products Engineering and Technology Research Center of Wuhan City, College of Food Science and Engineering,Wuhan Polytechnic University;
关键词：
fish bone;;collagen peptide;;chelated calcium
摘  要：
In order to achieve value-added utilization of byproducts of freshwater fish processing and simultaneously reduce environmental pollution and resource waste, silver carp bone was used as the raw material to prepare calcium-chelating collagen polypeptides. Under given conditions, calcium binding capacity and chelated calcium content were investigated as a function of reaction temperature, mass ratio between bone collagen polypeptides and calcium chloride(P/C), time and pH. On the basis of the results of single-factor experiments, the four reaction parameters were optimized by a fourfactor quadratic orthogonal rotational combination design to be 42 ℃, 38 min, a P/C ratio of 2.1:1 and pH 6.8, yielding a calcium binding capacity of 80.4% and a chelated calcium content of 12.1%. Amino acid composition analysis showed that the calcium-chelating collagen polypeptides obtained contained 61.03% amino acids in total and had typical amino acid composition characteristics. Infrared spectroscopic analysis and scanning electron microscopy observation confirmed the chelating reaction between calcium ion and collagen polypeptides by ionic bonding, coordination or adsorption.

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