大鲵肌肉与皮中胶原蛋白比较研究

Comparative Study on Collagen in Muscle and Skin of Giant Salamander

针对大鲵肉中肌基质蛋白和大鲵皮提取的胶原蛋白基础特性进行比较研究。采用酸法、胃蛋白酶法提取大鲵肌基质蛋白和大鲵皮中的胶原蛋白,测定胶原蛋白的分子质量、光谱特性、羟脯氨酸含量、微观结构与黏度。结果表明:大鲵皮、大鲵肉中肌基质蛋白的酸溶性胶原蛋白提取率分别达18.29%和7.08%,酶提胶原蛋白提取率分别为25.67%和18.65%;酸提大鲵皮、大鲵肌基质蛋白中胶原蛋白羟脯氨酸含量分别为(16.05±0.16)%和(10.49±0.42)%,酶提分别为(18.04±0.08)%和(8.67±0.12)%;酸提与酶提胶原蛋白紫外光谱及红外光谱特性基本相似,酸提大鲵皮胶原蛋白的种类比肌基质蛋白中提取的胶原蛋白种类更多,酶提大鲵皮中胶原蛋白电泳条带比肌基质蛋白中提取的胶原蛋白条带更为清晰,但分子质量基本一致;扫描电子显微镜观察结果表明,酸提的2种来源胶原蛋白网状结构较酶提更为完整;2种来源的胶原蛋白黏度存在显著差异(P<0.05)。大鲵肉中肌基质蛋白与大鲵皮胶原蛋白特性相同,可作为补充胶原蛋白制品及化妆品原料进行开发。

In this paper,the basic properties of collagens extracted from the muscle matrix protein and skin of giant salamander were evaluated and compared with each other.Acetic acid treatment followed by pepsin hydrolysis was used to extract collagen,and the molecular mass,spectral characteristics,hydroxyproline content,microstructure and viscosity of the collagens were determined.The results showed that the extraction yields of acid-soluble collagen from the skin and muscle matrix protein were 18.29%and 7.08%,and the extraction yields of collagen from the resulting residues with pepsin were 25.67%and 18.65%,respectively.The content of hydroxyproline was(16.05±0.16)%and(10.49±0.42)%for the acidsoluble collagens from the skin and muscle matrix protein,and(18.04±0.08)%and(8.67±0.12)%for the pepsin-extracted collagens,respectively.The ultraviolet and infrared spectral characteristics of the acid-extracted collagens were basically similar to those of the enzyme-extracted collagens,and more types of acid-extracted collagen were extracted from the skin than from the muscle matrix protein.The enzyme-extracted collagen from the skin showed more clear electrophoretic bands than that from the muscle matrix protein,but the molecular masses of them were similar to each other.Scanning electron microscopic(SEM)observation demonstrated that the reticular structure of acid-extracted collagens from both sources was more complete than that of enzyme-extracted collagens.A significant difference was found in the viscosity of collagens from the two sources(P<0.05),despite having the same properties as each other.Hence,they can be developed as raw materials for collagen supplement and cosmetics.