Isolation and Characterization of Acid Soluble Collagen from the Skin ofAfrican Catfish (Clarias gariepinus), Salmon (Salmo salar) and Baltic Cod (Gadus morhua)

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

Abstract

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.
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
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。
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