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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，在加热过程中负责鱼肉凝胶的形成。这种凝胶形成能力在很大程度上依赖于鱼类物种，但涉及这种物种特异性的机制仍不清楚。本研究旨在提高鱼脯制品的质量，白花鱼的凝胶形成模式与大眼鳕鱼不同，前者的质量明显好于后者。在此基础上，通过基因克隆的方法，测定了白花鱼和大眼鳗肌球蛋白重链亚基的一级结构，分别为1,930和1,937。在20~30℃范围内，白鱼鱼肉凝胶形成较慢，40℃以上时凝胶形成较快。经cDNA克隆确定其一级结构的原肌球蛋白与兔α原肌球蛋白具有较高的氨基酸序列同源性。以白花鱼为原料制备了肌球蛋白及其杆，并对其进行了粘弹性测试。凝胶形成的参数储能模数(G‘)在30~42℃时增大，42~48℃时减小，48~55℃时再次增大。L-肌球蛋白是用基因工程方法在大肠杆菌中重组大白鱼生产的，它是C端肌球蛋白棒的一半区域。差示扫描量热法(DS-C)显示重组LMM在31.7℃处有吸热峰，这是由于CD光谱证实了α-螺旋的展开。