[关键词]
[摘要]
为提高水产加工副产品的高值化利用,本文以资源丰富且相对集中的一种淡水产品加工下脚料-胡子鲶鱼皮为原料,在4 ℃条件下,利用酸提法从鲶鱼皮中提取酸溶性胶原蛋白(ASC),并对其进行相应的理化性质研究。通过测定羟脯氨酸含量得出了该鱼皮胶原蛋白的提取率(20.32%),氨基酸组成分析得到含量最丰富的氨基酸是甘氨酸(32.59%)表明样品符合Ⅰ型胶原蛋白的氨基酸特点。SDS-PAGE电泳和紫外分析图谱表明样品为Ⅰ型胶原蛋白,且样品提取纯度较好。傅里叶变换红外光谱(FT-IR)表明该酸溶性胶原蛋白保留了天然的三螺旋结构。热变性温度(Td,26 ℃)和热收缩温度(Ts,53.01 ℃)的测定结果均显示,这种鲶鱼皮酸溶性胶原蛋白的热稳定性低于哺乳动物。X-射线衍射图谱显示了胶原蛋白分子的内部结构特点。
[Key word]
[Abstract]
Fish skin of Clarias fuscus was a by-product of freshwater aquatic products processing, which is rich in resources. To improve the utilization of aquatic by-products, the fish skin of Clarias fuscus was used as raw materials for acid-soluble collagen (ASC) extraction at 4 ℃. It’s the physicochemical of the extracts was then studied. The hydroxyproline experiment showed that the extraction yield of ASC reached 20.32%. The sample met the characteristics of type I collagen with the most abundant amino acid of glycine (32.59%) by analysis of amino acid compositions. SDS-PAGE and ultraviolet-visible (UV-Vis) spectra identified the sample was of a type I collagen protein with high purity. Fourier transform infrared (FT-IR) spectra of ASC suggested that the protein presented in the triple helix structure. The denature temperature (Td, 26 ℃) and shrinkage temperature (Ts, 53.01 ℃) showed that the thermal stability of the collagen was lower than collagen from mammalian. X-ray diffraction diagram showed the internal structure of the collagen molecules from Skin of Clarias fuscus.
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[基金项目]
海洋公益性专项(201205027);中国博士后面上基金(2012M511549)