College of Food Science and Engineering, Ocean University of China, No.5, Yu Shan Road, Qingdao, Shandong Province 266003, PR China.
College of Food Science and Engineering, Ocean University of China, No.5, Yu Shan Road, Qingdao, Shandong Province 266003, PR China; Laboratory for Marine Drugs and Bioproducts, Qingdao National Laboratory for Marine Science and Technology, Qingdao, Shandong Province 266237, PR China.
Food Chem. 2020 Nov 30;331:127340. doi: 10.1016/j.foodchem.2020.127340. Epub 2020 Jun 13.
Acid-soluble collagen (ASC) and pepsin-soluble collagen (PSC) were extracted and purified from the cartilages of skate and sturgeon. Their typical structure and physicochemical properties were evaluated by circular dichroism (CD), X-ray diffraction (XRD), and so on. Results showed that the extracted collagen was likely identified as collagen-II composed of three α-chains (135 kDa), with the typical peptide sequence of Gly-X-Y. It showed the collagen retained the native and intact triple helical structure, and its intensity ratio of the positive and negative absorption peaks (Rpn) was 0.19-0.25. In addition, the extracted collagen exhibited obvious self-assembly behavior with the concentration above 0.3 mg/mL, the adjustment of pH 7.4-7.6 and the NaCl concentration of 120 mmol/L. The critical aggregate mass concentrations of pepsin-soluble collagens from skate and sturgeon were 0.93 and 0.86 g/L, respectively. Therefore, collagens from skate and sturgeon cartilages have potential commercial application.
从软骨鱼和鲟鱼的软骨中提取并纯化了酸溶性胶原蛋白（ASC）和胃蛋白酶溶性胶原蛋白（PSC）。通过圆二色性（CD）、X 射线衍射（XRD）等方法评估了它们的典型结构和物理化学性质。结果表明，提取的胶原蛋白可能被鉴定为由三条α链（135 kDa）组成的 II 型胶原蛋白，具有甘氨酸-脯氨酸-羟脯氨酸（Gly-X-Y）的典型肽序列。它表明胶原蛋白保留了天然完整的三螺旋结构，其正吸收峰和负吸收峰的强度比（Rpn）为 0.19-0.25。此外，当浓度高于 0.3 mg/mL、pH 值为 7.4-7.6 以及 NaCl 浓度为 120 mmol/L 时，提取的胶原蛋白表现出明显的自组装行为。来自软骨鱼和鲟鱼软骨的胃蛋白酶溶性胶原蛋白的临界聚集质量浓度分别为 0.93 和 0.86 g/L。因此，软骨鱼和鲟鱼软骨中的胶原蛋白具有潜在的商业应用价值。
