食品科学 ›› 2022, Vol. 43 ›› Issue (23): 194-201.doi: 10.7506/spkx1002-6630-20220512-156

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低温冷链贮藏对鱼糜凝胶化学作用力和肌原纤维蛋白结构及功能特性的影响

陈旭,余璐涵,蔡茜茜,吴金鸿,刘永乐,黄建联,汪少芸   

  1. (1.福州大学生物科学与工程学院,福建 福州 350108;2.福建省冷冻调理水产品加工重点实验室,福建 厦门 361022;3.上海交通大学农业与生物学院,上海 200204;4.长沙理工大学食品与生物工程学院,湖南 长沙 410114;5.安井食品集团股份有限公司,福建 厦门 361022)
  • 出版日期:2022-12-15 发布日期:2022-12-28
  • 基金资助:
    国家自然科学基金联合基金项目(U1905202);国家自然科学基金面上项目(31972017); 厦门市海洋与渔业发展专项资金项目(21CZP006HJ04)

Effect of Cold Chain Storage on Chemical Interactions of Surimi Gel and Structural and Functional Properties of Myofibrillar Protein

CHEN Xu, YU Luhan, CAI Xixi, WU Jinhong, LIU Yongle, HUANG Jianlian, WANG Shaoyun   

  1. (1. College of Biological Science and Engineering, Fuzhou University, Fuzhou 350108, China; 2. Fujian Provincial Key Laboratory of Frozen Processed Aquatic Products, Xiamen 361022, China; 3. School of Agriculture and Biology, Shanghai Jiao Tong University, Shanghai 200204, China; 4. School of Food and Bioengineering, Changsha University of Science and Technology, Changsha 410114, China; 5. Anjoy Food Group Co., Ltd., Xiamen 361022, China)
  • Online:2022-12-15 Published:2022-12-28

摘要: 为研究低温冷链对鱼糜肌原纤维蛋白和凝胶化学作用力的影响。本实验以鱼糜为研究对象,测定了低温冷链贮藏时间对肌原纤维蛋白功能基团、二级结构、三级结构和凝胶化学作用力的影响,并进一步通过主成分分析和相关性分析探究凝胶化学作用力与肌原纤维蛋白之间的关系。结果表明,贮藏过程中鱼糜盐溶性蛋白含量、Ca2+-ATPase活力和总巯基含量呈下降趋势,而羰基含量上升。此外,蛋白质二级结构由有序向无序转变,肌原纤维蛋白荧光强度下降,说明蛋白极性环境发生改变。揭示了肌原纤维蛋白中的活性基团与凝胶化学作用力的形成密切相关。因此,在贮藏初期防止蛋白氧化和冷冻变性是维持鱼糜凝胶化学作用力,保持鱼糜凝胶特性的有效途径。本研究可为鱼糜在低温冷链贮藏过程中的品质保持提供基础理论支持。

关键词: 鱼糜凝胶;肌原纤维蛋白;化学作用力;蛋白质结构;低温冷链

Abstract: In order to study the effect of cold chain storage on the structural and functional properties of myofibrillar protein and the chemical interactions of surimi gel, the changes in the functional groups and secondary and tertiary structure of myofibrillar protein and the chemical interactions of surimi gel were investigated as a function of cold chain storage time, and the relationship between chemical interactions and myofibrillar protein was evaluated by principal component analysis (PCA) and correlation analysis. Results showed that the salt-soluble protein content, Ca2+-ATPase activity and total sulfhydryl content in surimi gel decreased, while the carbonyl content increased during storage.?In addition, the secondary structures of myofibrillar protein transformed from an ordered to a disordered state, and the fluorescence intensity decreased, indicating changes in the polar environment of the protein. These findings demonstrate that the active groups in myofibrillar protein are closely related to the formation of gel chemical forces.?Therefore, preventing protein oxidation and freeze denaturation at the initial stage of storage is an effective way to maintain the chemical interactions of surimi gel and the gel characteristics. This study can provide basic theoretical support for the quality maintenance of surimi during cold chain storage.

Key words: surimi gel; myofibrillar protein; chemical interactions; protein structure; cold chain

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