胡子鲶鱼皮酸溶性胶原蛋白的理化性质研究

Physicochemical Properties of Acid-soluble Collagen from Skin of Clarias fuscus

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。

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.