非洲鲶鱼(Clarias gariepinus)、鲑鱼(Salmo salar)和波罗的海鳕鱼(Gadus morhua)皮肤中酸溶性胶原蛋白的分离与鉴定

R. Tylingo, Szymon Mania, A. Panek, RafaÅ PiÄtek, Roman PawÅowicz
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引用次数: 26

摘要

从非洲鲶鱼(Clarias gariepinus)、鲑鱼(Salmo salar)和波罗的海鳕鱼(Gadus morhua)的鱼皮中提取并鉴定了酸溶性胶原蛋白(ASC)。ASC的提取率分别为75%、73%和68%。非洲鲶鱼的ASC(29.3°C和100.0°C)显著高于鲑鱼和波罗的海鳕鱼(20.6°C和90.5°C);15.2°C和86.7°C),通过差示扫描量热法评估。SDS-PAGE图谱显示,每个ASC均为I型胶原,由α1和α2两条不同的α链以及β组分组成。所有胶原蛋白的FTIR光谱表明,它们的整体化学成分非常相似。鱼皮胶原蛋白易于制备,是一种可能用于工业规模的资源。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Isolation and Characterization of Acid Soluble Collagen from the Skin ofAfrican Catfish (Clarias gariepinus), Salmon (Salmo salar) and Baltic Cod (Gadus morhua)
Acid-soluble collagen (ASC) from the fish skin of African catfish (Clarias gariepinus), Salmon (Salmo salar) and Baltic cod (Gadus morhua) was extracted and characterized. The ASC extraction yield was 75%, 73% and 68%, respectively. The denaturation and melting temperatures of African catfish ASC (29.3°C and 100.0°C) were significantly higher than ASC of Salmon and Baltic cod (20.6°C and 90.5°C; 15.2°C and 86.7°C, respectively), assessed by differential scanning calorimetry. The SDS-PAGE profile showed that each of tested ASC was the type I collagen and consisted of two different α chains, α1 and α2, as well as a β component. The FTIR spectra of all collagens indicate that the overall their chemical compositions are quite similar. The fish skin collagen is easy to prepare and represents a possible resource for use on industrial scale.
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