Graduate School of Fisheries Sciences, Hokkaido University, 3-1-1 Minato-cho, Hakodate, Hokkaido 041-8611, Japan.
Graduate School of Fisheries Sciences, Hokkaido University, 3-1-1 Minato-cho, Hakodate, Hokkaido 041-8611, Japan.
Food Chem. 2014 Oct 1;160:305-12. doi: 10.1016/j.foodchem.2014.03.075. Epub 2014 Mar 24.
Collagens purified from Bester sturgeon organs were characterised biochemically, and their fibril-forming abilities and fibril morphologies formed in vitro clarified. Yields of collagens were 2.1%, 11.9%, 0.4%, 18.1%, 0.4%, 0.8% and 0.03% (collagen dry weight/tissue wet weight) from scales, skin, muscle, swim bladder, digestive tract, notochord and snout cartilage, respectively. Using SDS-PAGE and amino acid composition analyses, collagens from scales, skin, muscle, the swim bladder and digestive tract were characterised as type I, and collagens from the notochord and snout cartilage as type II. Denaturation temperatures of the collagens, measured using circular dichroism, were 29.6, 26.8, 29.0, 32.9, 31.6 and 36.3 °C in scales, skin, muscle, swim bladder, digestive tract, and notochord, respectively. For fibril formation, swim bladder and skin collagen showed a more rapid rate of increase in turbidity, a shorter time to attain the maximum turbidity, and formed thicker fibrils compared with porcine tendon type I collagen.
从白鲟器官中提取的胶原蛋白进行了生化特性分析，并阐明了其在体外形成纤维的能力和纤维形态。从鳞片、皮肤、肌肉、鱼鳔、消化道、脊索和鼻软骨中分别获得胶原蛋白的产率为 2.1%、11.9%、0.4%、18.1%、0.4%、0.8%和 0.03%（胶原蛋白干重/组织湿重）。通过 SDS-PAGE 和氨基酸组成分析，鳞片、皮肤、肌肉、鱼鳔和消化道中的胶原蛋白被鉴定为 I 型，而脊索和鼻软骨中的胶原蛋白被鉴定为 II 型。使用圆二色性测量的胶原蛋白变性温度分别为鳞片、皮肤、肌肉、鱼鳔、消化道和脊索中的 29.6、26.8、29.0、32.9、31.6 和 36.3°C。对于纤维形成，与猪肌腱 I 型胶原蛋白相比，鱼鳔和皮肤胶原蛋白的浊度增加更快，达到最大浊度的时间更短，形成的纤维更厚。
