School of Medical Science and Technology, Indian Institute of Technology, Kharagpur 721302, India.
Bioresour Technol. 2010 May;101(10):3737-42. doi: 10.1016/j.biortech.2009.12.133. Epub 2010 Jan 29.
Collagen is the most abundant protein found in animal body and widely used for biomedical and pharmaceutical applications. However, its applicability is severely limited due to high cost. Fish processing waste, which otherwise cause serious environmental pollution, is a promising cost effective collagen source. In the present study, collagen was isolated from scales of Labeo rohita (Rohu) and Catla catla (Catla). It is first time that these species are used as sources of collagen. Thermo-gravimetric analysis (TGA) revealed maximum demineralization achieved after 48h of EDTA treatment of intact scale. The isolated protein was confirmed as collagen by different physico-chemical techniques like FTIR, SDS-PAGE, and CD. Further amino acid analysis corroborates isolation of type I collagen. A major characteristic of obtained collagen was found to have denaturation temperature (T(d)) of 36.5 degrees C, which is promising as an advantage for biomedical application due to closeness in T(d) to mammalian collagen.
胶原蛋白是动物体内最丰富的蛋白质，广泛用于生物医学和制药应用。然而，由于成本高，其适用性受到严重限制。鱼类加工废物本来会造成严重的环境污染，但却是一种有前途的具有成本效益的胶原蛋白来源。本研究从罗非鱼（Rohu）和印度鲃（Catla）的鳞片中分离出胶原蛋白。这是首次将这些物种用作胶原蛋白的来源。热重分析（TGA）表明，在用 EDTA 处理完整鳞片 48 小时后，达到了最大的脱矿化效果。通过不同的物理化学技术，如傅里叶变换红外光谱（FTIR）、SDS-PAGE 和 CD，证实了分离出的蛋白质为胶原蛋白。进一步的氨基酸分析证实了 I 型胶原蛋白的分离。所获得的胶原蛋白的一个主要特征是变性温度（T(d)）为 36.5 摄氏度，由于与哺乳动物胶原蛋白的 T(d)接近，这对于生物医学应用是一个有前景的优势。
