胡远辉,廖慧琦,陆益钡,杨巨鹏,张慧恩,洪梦蓉,杨 华.液氮冻结对养殖大黄鱼肌原纤维蛋白结构的影响[J].食品安全质量检测学报,2020,11(22):8260-8266
液氮冻结对养殖大黄鱼肌原纤维蛋白结构的影响
Effects of liquid nitrogen freezing nitrogen on the structure of myofibrillar protein in cultured large yellow croaker (Pseudosciaena crocea)
投稿时间:2020-08-01  修订日期:2020-10-28
DOI:
中文关键词:  液氮冻结  养殖大黄鱼  肌原纤维蛋白  结构特性
英文关键词:liquid nitrogen freezing  cultured large yellow croaker  myofibrillar protein  structural characteristics
基金项目:浙江省重点研发计划项目(2019C02071)、宁波市基金项目(2019A610431)
作者单位
胡远辉 浙江万里学院生物与环境学院 
廖慧琦 浙江万里学院生物与环境学院 
陆益钡 浙江万里学院生物与环境学院 
杨巨鹏 浙江万里学院生物与环境学院 
张慧恩 浙江万里学院生物与环境学院 
洪梦蓉 浙江万里学院生物与环境学院 
杨 华 浙江万里学院生物与环境学院 
AuthorInstitution
HU Yuan-Hui School of Biology and the Environment, Zhejiang Wanli University 
LIAO Hui-Qi School of Biology and the Environment, Zhejiang Wanli University 
LU Yi-Bei School of Biology and the Environment, Zhejiang Wanli University 
YANG Ju-Peng School of Biology and the Environment, Zhejiang Wanli University 
ZHANG Hui-En School of Biology and the Environment, Zhejiang Wanli University 
HONG Meng-Rong School of Biology and the Environment, Zhejiang Wanli University 
YANG Hua School of Biology and the Environment, Zhejiang Wanli University 
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中文摘要:
      目的 探究液氮冻结对大黄鱼肌原纤维蛋白结构的影响。方法 通过荧光分光光度法、傅里叶红外法、圆二色光谱法、激光拉曼光谱法等分析, 探究液氮冻结对大黄鱼肉肌原纤维蛋白结构的变化。结果 冻结后大黄鱼肉肌原纤维蛋白表面疏水性上升, 巯基含量下降, 蛋白质二、三级结构在冻结下发生改变, α-螺旋的含量被下降, 转化为β-折叠和无规卷曲, 影响肽链结合的紧密性。结论 蛋白结构的变化影响大黄鱼肉中肌原纤维蛋白的二、三级结构, 进而影响鱼肉的品质特性。
英文摘要:
      Objective To investigate the effects of liquid nitrogen freezing on myofibrillar protein structure in cultured large yellow croaker. Methods Fluorescence spectrophotometry, Fourier infrared spectroscopy, circular dichroism, laser Raman spectroscopy and other methods were used to explore the changes of liquid nitrogen freezing on the structure of myofibrillar protein of large yellow croaker. Results After freezing, the surface hydrophobicity of myofibrillar protein in cultured large yellow croaker increased, the sulfhydryl content decreased, the secondary and tertiary structure of the protein changed under freezing, and the α-helix content decreased and converted to β-Folding and random coiling, mainly affecting the tightness of peptide chain binding. Conclusion The changes of protein structure affect the secondary and tertiary structures of myofibrillar protein structure in cultured large yellow croaker, and then affect the quality characteristics of fish.
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