Identification and Utilization of the Region Responsible for Fish Meat Gel Formation with Respect to Improvements of the Quality for Surimi-based Products

鱼肉凝胶形成区域的识别和利用与提高鱼糜产品的质量

基本信息

批准号：
10356007
负责人：
WATABE Shugo
金额：
$ 20.1万
依托单位：
THE UNIVERSITY OF TOKYO
依托单位国家：
日本
项目类别：
Grant-in-Aid for Scientific Research (A).
财政年份：
1998
资助国家：
日本
起止时间：
1998 至 2000
项目状态：
已结题

项目摘要

Myosin is a major muscle protein and responsible for fish meat gel formation in accompany with heat treatment. Such gel forming ability is dependent largely on fish species, but mechanisms involved in such species-specificity have remained unknown. This research project was performed aiming the improvement of quality for surimi-based products.The gel forming pattern for white croaker Pennahia argentata was different from that of walleye pollack Theragra chalcograma, the former quality being much better than that of the latter. Then, the primary structures of myosin heavy chain subunit was determined for white croaker and walleye pollack by cDNA cloning, and were found to contain 1,930 and 1,937, respectively. Gel formation of white croaker meat was slow at 20 to 30℃ and high and effective over 40℃ in white croaker meat. Tropomyosin from white croaker which was determined for its primary structure by cDNA cloning, showed high amino acid sequence identity to rabbit alpha tropomyosin. Myosin and its rod were prepared from white croaker and subjected to viscoelastic measurements. The storage modulus (G'), a parameter for gel formation, was increased at 30 to 42℃, decreased at 42 to 48℃, and increased again at 48 to 55℃. L-meromyosin (LMM), a half region of myosin rod in the C-terminal side, was produced by a genetically engineering method using recombinant DNA in E.coli for white croaker. Recombinant LMM showed endothermic peak at 31.7℃ in Differential scanning calorimetry (DS) C runs due to unfolding of alpha helix that was demonstrated by CD spectroscopy.

肌球蛋白是一种主要的肌肉蛋白质，并负责热处理的鱼肉凝胶形成。这种凝胶形成能力在很大程度上取决于鱼类，但是这种物种特异性涉及的机制尚不清楚。该研究项目的目的是针对基于Surimi的产品的质量提高。白色鳄鱼pennahia Argentata的凝胶形成模式与Walleye Pollack Theragra Chalcogragr的不同，形式的质量要比后者好得多。然后，通过cDNA克隆确定了肌球蛋白重链亚基的主要结构，并分别含有1,930和1,937。白色鳄鱼肉的凝胶形成在20至30℃时缓慢，高高且有效40℃，在白色鳄鱼肉中。白色鳄鱼皮的真菌类球菌通过cDNA克隆确定其主要结构，显示出高氨基酸序列的身份，对兔α-肌球蛋白。肌球蛋白及其杆是从白色鳄鱼制成的，并进行了粘弹性测量。储存模量（G'）是凝胶形成的参数，在30至42℃时增加，在42至48℃下减少，并在48至55°时再次增加。 L-肌球蛋白（LMM）是C末端的肌球蛋白杆的一半区域，是通过使用重组DNA在E.Coli中用于白色Croaker的基因工程方法的。重组LMM在差异扫描量热法（DS）C中显示在31.7时的吸热峰，这是由于CD光谱证明的α螺旋的展开而导致的。