从鲢鱼皮、鱼鳞中分别提取并纯化酸溶性和酶溶性胶原，得到四种不同的胶原，并分析四种胶原在分子组成、空间结构、热稳定性等方面的异同，为基于淡水鱼来源的胶原材料的构建提供理论依据。研究发现，四种胶原的紫外图谱、红外图谱和圆二色谱图相似，即空间结构类似，均具有天然的三股螺旋的空间构象，符合典型的Ⅰ型胶原的特点；四种胶原的氨基酸组成和比例接近；酸溶性胶原（ASC）的分子结构中二聚体β链含量多，且α1链和α3链的分子量相同，酶溶性胶原（PSC）的分子结构中二聚体β链含量少，三条α链区分明显，且鱼皮PSC和鱼鳞PSC的α链分子量分布不同；ASC溶液的粘度大于PSC，鱼皮ASC溶液的粘度大于鱼鳞ASC；四种鲢鱼胶原的热变性温度不同，即用不同方法从不同部位提取的胶原热稳定性有差异。

The acid-soluble collagen (ASC) and pepsin-soluble collagen (PSC) were extracted from the skin or scale of Hypophthalmichthys molitrix, and four different collagen samples were obtained. The molecular structure and thermostability of the four collagen samples were compared, and this study provides a theoretical basis for the preparation of collagen materials from fresh fish. The study shows that the four collagen samples showed similar ultraviolet absorption spectra, FT-IR spectra, and circular dichroism spectra. Their spatial structures were similar, and they showed a natural triple helical conformation, matching the typical characteristics of type I collagen. The amino acid composition and proportion of the four collagen samples are quite similar. In the molecular structure of ASC, the content of dimeric (β-chains) subunits was relatively high, and the molecular weights of the α1 and α2 chains were the same. In the molecular structure of PSC, the content of dimeric (β-chains) subunits was relatively low. Significant differences were observed in three of the α chains, and α chain distributions in the collagen samples from PSC skin and PSC scale were different. The viscosity of ASC collagen solutions was greater than that of PSC collagen solutions, and the viscosity of the ASC skin collagen solution was greater than that of the ASC scale collagen solution. Finally, the thermal denaturation temperatures of the four H. molitrix collagens were different; that is, differences were present in the thermal stability of the collagen samples extracted from different parts by different methods.

国家现代农业产业技术体系建设专项(CARS-46-23)