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中国精品科技期刊2020
王园园, 张靓, 周鹏. 太湖白鱼中胶原蛋白的提取及其理化性质分析[J]. 新宝登录入口(中国)有限公司, 2017, (18): 45-49. DOI: 10.13386/j.issn1002-0306.2017.18.009
引用本文: 王园园, 张靓, 周鹏. 太湖白鱼中胶原蛋白的提取及其理化性质分析[J]. 新宝登录入口(中国)有限公司, 2017, (18): 45-49. DOI: 10.13386/j.issn1002-0306.2017.18.009
WANG Yuan-yuan, ZHANG Liang, ZHOU Peng. Extraction and physicochemical properties of collagen from white fish of Taihu Lake ( Erythroculter ilishaeformis)[J]. Science and Technology of Food Industry, 2017, (18): 45-49. DOI: 10.13386/j.issn1002-0306.2017.18.009
Citation: WANG Yuan-yuan, ZHANG Liang, ZHOU Peng. Extraction and physicochemical properties of collagen from white fish of Taihu Lake ( Erythroculter ilishaeformis)[J]. Science and Technology of Food Industry, 2017, (18): 45-49. DOI: 10.13386/j.issn1002-0306.2017.18.009

太湖白鱼中胶原蛋白的提取及其理化性质分析

Extraction and physicochemical properties of collagen from white fish of Taihu Lake ( Erythroculter ilishaeformis)

  • 摘要: 从白鱼鱼鳍、鱼鳞、鱼皮、鱼肉、鱼骨、鱼鳔中提取胶原蛋白,研究不同p H条件下胶原蛋白溶解度的变化。分别运用高效液相色谱法、十二烷基硫酸钠-聚丙烯酰胺凝胶电泳、酶解肽图分析、差示量热扫描法分析白鱼各部位提取的胶原蛋白的组成、结构以及理化性质。结果表明,白鱼各部位的胶原蛋白在酸性(p H34)条件下具有较好的溶解性,中碱性条件下溶解度骤降。在p H4条件下,鱼皮、鱼鳔中胶原蛋白的提取率高于其他部位,分别达到18.80%和15.95%。白鱼各部位胶原蛋白具有相似的氨基酸组成,蛋白分子中含有1/3左右的甘氨酸,脯氨酸和羟脯氨酸的含量在154.2199.0残基/1000个残基之间,亚基分子量相似,存在两条不同的α链(α1和α2),主要为Ⅰ型胶原蛋白,变性温度在34.1636.40℃之间。白鱼各部位提取的胶原蛋白在组成、结构和理化性质上具有良好的相似性。 

     

    Abstract: Collagens were extracted from the fin, scale, skin, muscle, bone and swim bladder of white fish at different p H.HPLC, SDS-PAGE, peptide mapping and DSC were used to investigate the compositions and physiochemical properties of the collagens, which were extracted from different parts of white fish.The results showed that, collagens could be more soluble in the acidic p H range from 3 ~ 4, while the solubility decreased under neutral and alkaline condition. Extraction ratios of collagens from skin and swim bladder were 18.80% and 15.95% respectively, which were higher than those of other white fish parts.Similar peptide maps of collagens extracted from different parts of white fish indicated that primary structures of these collagens were quite similar in terms of amino acid sequence.Nearly 1/3 of the total amino acid was Gly, and a high level of Pro and Hyp up to 154.2199.0 residues/1000 residues.The collagens from all parts of white fish were comprised of two kinds α chains ( α1and α2) and classified as type I collagens.The denaturation temperatures of these collagens were between 34.1636.40 ℃.The collagens extracted from different parts of white fish had good similarity in composition, structure and physicochemical properties.

     

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