Isolation and characterization of fish scale collagen of higher thermal stability
Isolation and characterization of fish scale collagen of higher thermal stability
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DOI：
10.1016/j.biortech.2009.12.133
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发表时间：
2010-05-01
影响因子：
11.4
通讯作者：
Dhara, Santanu
中科院分区：
文献类型：
--
作者：
Pati, Falguni;Adhikari, Basudam;Dhara, Santanu
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领域。然而，由于成本高，其适用性受到严重限制。鱼类加工废弃物会造成严重的环境污染，但却是一种很有前途的具有成本效益的胶原蛋白来源。本研究从野Labeo rohita（Rohu）和Catla catla（Catla）鳞片中提取胶原蛋白。这是首次将这些物种用作胶原蛋白的来源。热重分析（TGA）显示最大的脱矿物质后，48小时的EDTA处理的完整的规模。分离的蛋白质经FTIR、SDS-PAGE、CD等理化技术鉴定为胶原蛋白。进一步的氨基酸分析证实了I型胶原蛋白的分离。发现所获得的胶原蛋白的主要特征是具有36.5 ℃的变性温度（T-d），由于T-d与哺乳动物胶原蛋白接近，这对于生物医学应用是有希望的优势。(C)2010爱思唯尔有限公司版权所有。
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 48 h 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. (C) 2010 Elsevier Ltd. All rights reserved.