文章摘要
汪之和,朱孔辉,施文正,郭丰红.鳊鱼鱼糜蛋白质结构与凝胶特性关系的研究[J].水产学报,2010,34(5):814~819
鳊鱼鱼糜蛋白质结构与凝胶特性关系的研究
Studies on the protein structure and characteristics of gel strength of Parabramis pekinensis surimi
投稿时间:2009-11-19  修订日期:2010-01-30
DOI:10.3724/SP.J.1231.2010.06715
中文关键词:   鱼糜  化学作用力  蛋白质构象
英文关键词: Parabramis pekinensis  surimi  chemical interactions  protein conformation
基金项目:上海市农委项目
作者单位E-mail
汪之和 上海海洋大学 zhwang@shou.edu.cn 
朱孔辉 上海海洋大学食品学院  
施文正 上海海洋大学食品学院  
郭丰红 上海海洋大学食品学院  
摘要点击次数: 1981
全文下载次数: 1942
中文摘要:
      蛋白质对于鱼糜凝胶形成具有重要作用,通过研究鳊鱼鱼糜贮藏过程中肌球蛋白化学作用力、激光拉曼光谱等的变化探讨蛋白质结构对鱼糜凝胶形成的影响。结果发现,鱼糜在-80 ℃、-20 ℃冻藏过程中,肌球蛋白含量、离子键、氢键与疏水相互作用含量呈现先快后慢的二段式下降趋势,与其凝胶强度变化趋势一致;在0 ℃和5 ℃贮藏过程中,肌球蛋白含量、离子键和氢键含量呈不断下降的趋势,与凝胶强度变化趋势基本一致,而疏水相互作用为先增加后减少,由此可见,肌球蛋白含量、离子键和氢键含量在维持鱼糜蛋白高级结构上起着重要的作用。激光拉曼光谱结果显示α-螺旋结构是维持鳊鱼糜蛋白质网状结构的主要构象,在贮藏过程中,部分α-螺旋结构转变成无规卷曲,使包埋于肌球蛋白分子内的疏水性残基暴露于分子表面,进而发生蛋白变性;贮藏温度越高,无规卷曲结构越多,蛋白变性程度越大,表现在凝胶强度降低越多。鱼糜贮藏过程中蛋白质结构变化的研究对于阐明鱼糜凝胶形成机理和防止鱼糜蛋白变性具有一定意义。
英文摘要:
      Protein plays an important role in the gel forming of surimi. The effects of protein structure on the gel formation of surimi were studied through the changes of myosin chemical interactions and laser Raman spectroscopy during the Parabramis pekinensis surimi storage. The results showed that the myosin contents, ionic bonds, hydrogen bonds and hydrophobic bonds of surimi decreased fast at first and then slowly as well as the changes of gel strength during storage at the temperature of -80 ℃ and -20 ℃. The myosin contents, ionic bonds and hydrogen bonds of surimi declined directly during storage at the temperature of 0 ℃ and 5 ℃, while the hydrophobic bond increased at first and then decreased. Thus, It can be concluded that myosin contents, ionic bonds and hydrogen bonds play important roles in maintaining the complex high level structure of surimi. According to the Laser Raman spectroscopy, α-helix structure is the major conformation maintaining protein network structure of Parabramis pekinensis surimi. Part of α-helix of myosin changed into random coil structure during the storage. When α-helix structure turned into random coil partly, the hydrophobic residues embedded in myosin molecules were exposed to the surface of molecules as the protein denatured. The higher the storage temperature, the more content of random coil structure and the greater the degree of protein denaturation, which reflected in the gel strength decreased more. The study of surimi protein structural changes during the storage of surimi clarifies the formation mechanism and the prevention of surimi protein denaturation significantly. The correlation of surimi myosin chemical interactions, protein secondary structure and the ability of surimi gel forming could be continued in the future research.
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