Characterisation, Amino Acid Composition and Denaturation status of Acid Soluble Collagen from Catfish (Clarias gariepinus) Skin

A. Adejumo, L. Azeez, Ebenezer I. O. Ajayi, T. G. Atere, F. Aderibigbe, R. O. Adetoro
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引用次数: 1

Abstract

This study reported characterisation of acid-soluble collagen from the skin of freshwater catfish (Clarias gariepinus) by Fourier Transform Infra-Red spectroscopy (FTIR), scanning electron microscopy (SEM) and energy dispersive x-ray (EDX). Amino acid composition and denaturation temperature of the collagen were determined. Acid soluble collagen (ASC) from the skin of C. gariepinus produced a comparatively yield of 2.38% with all amide functional groups (Amide A, B, I, II and III) visible in the FTIR spectrum suggesting the intactness of triple helical structure of the collagen. The SEM of C. glariepinus, shows a mono-fibrillated irregularly arranged crystalline surface material having 24.46 % carbon, 11.72 % oxygen and 9.40 % nitrogen. The abundance of amino acids follows glycine > arginine > proline > alanine indicating the integrity of collagen and a non-disruptive method of extraction. The denaturation temperature (Td) of ASC was about 30 °C implying its usefulness in food and pharmaceutical industries.
鲶鱼(Clarias gariepinus)皮肤中酸溶性胶原蛋白的特性、氨基酸组成和变性状态
利用傅里叶变换红外光谱(FTIR)、扫描电子显微镜(SEM)和能量色散x射线(EDX)对淡水鲶鱼(Clarias gariepinus)皮肤中的酸溶性胶原蛋白进行了表征。测定胶原蛋白的氨基酸组成和变性温度。酸溶性胶原蛋白(ASC)产率为2.38%,在FTIR光谱中可见酰胺a、酰胺B、酰胺I、酰胺II和酰胺III,表明胶原蛋白具有完整的三螺旋结构。经扫描电镜观察,甘精晶体表面呈单纤原结构,碳含量为24.46%,氧含量为11.72%,氮含量为9.40%。氨基酸丰度依次为甘氨酸>精氨酸>脯氨酸>丙氨酸,表明胶原蛋白的完整性和非破坏性提取方法。ASC的变性温度(Td)约为30℃,表明其在食品和制药工业中的用途。
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