草鱼鱼鳞、鱼皮和鱼骨酸溶性胶原蛋白特性对比研究  

Comparative study on acid soluble collagen of grass carp fish scale, skin and bone

作　　者：瞿朝霞[1] 刘焱[1,2] 罗灿[1] 刘伦伦[1] 

机构地区：[1]湖南农业大学食品科学技术学院,湖南长沙410128 [2]湖南农业大学食品科学与生物技术湖南省重点实验室,湖南长沙410128

出　　处：《中国酿造》2014年第5期116-119,共4页China Brewing

基　　金：国家星火计划重大项目(2011GA770007);湖南省重大科技专项(2010FJ1007-2)

摘　　要：从草鱼鱼鳞、鱼皮和鱼骨中提取酸溶性胶原蛋白(ASC),对其特性进行对比分析。紫外光谱和电泳图谱结果显示,3种ASC紫外特征吸收峰出现位置与I型胶原蛋白紫外特征吸收峰出现的位置基本一致,分子结构都至少含有两条α链;傅里叶红外光谱显示,草鱼鱼鳞、鱼皮和鱼骨ASC在酰胺A带的N-H伸缩均以氢键形成缔合体,酰胺Ⅰ带和酰胺Ⅲ带的特征吸收峰表明鱼鳞和鱼骨ASC的α-螺旋结构保存较完整,鱼皮ASC的α-螺旋结构已经被破坏;3种ASC在热稳定性方面存在一定差异,热变性温度鱼骨ASC(34.5℃)>鱼皮ASC(32℃)>鱼鳞ASC(31℃),可能与胶原存在的组织和所处的环境有关。Comparative analysis on characteristics of acid soluble collagen （ASC） extracted from grass carp fish scale, skin and bone was conducted. The ultraviolet spectrum and electrophoresis showed that ultraviolet characteristics absorption peak positions of three kinds of ASC were consistent with type Ⅰ collagen, and the molecular structure containing at least two a-chains. The fourier infrared spectrum showed that N-H bonded with hydrogen forming hydrogen bond in amide A belt, and the amide Ⅰ belt and amide Ⅲ characteristic absorption peak showed that the α-helix structure of fish scale and fish bone ASC was relatively intact, and the α-helix structure of fish skin ASC was destroyed. The thermal denaturation temperature in order was fish bone ASC （34.5℃）, fish skin ASC （32.0℃）, fish scales ASC （31.0℃）, which may be related to the collagen organization and environment.

关 键 词：草鱼 酸溶性胶原蛋白 电泳 红外光谱 

分 类 号：TS254.1[轻工技术与工程—水产品加工及贮藏工程]