食品科学 ›› 2019, Vol. 40 ›› Issue (9): 61-67.doi: 10.7506/spkx1002-6630-20180409-113

• 基础研究 • 上一篇    下一篇

超高压处理对养殖大黄鱼肌原纤维蛋白结构的影响

张登科1,2,张慧恩2,朱艳杰2,杨巨鹏2,雷叶斯2,杨 华2,*,娄永江1,*   

  1. 1.宁波大学食品与药学学院,浙江 宁波 315800;2.浙江万里学院生物与环境学院,浙江 宁波 315100
  • 出版日期:2019-05-15 发布日期:2019-05-28
  • 基金资助:
    浙江省自然科学基金项目(LY17C200001);宁波市富民专项(2015C10018;2016C10009);浙江省“生物工程”重中之重学科学生创新计划项目(CX2017017)

Effect of High Hydrostatic Pressure Treatment on Myofibrillar Protein Structure of Cultured Large Yellow Croaker

ZHANG Dengke1,2, ZHANG Huien2, ZHU Yanjie2, YANG Jupeng2, LEI Yesi2, YANG Hua2,*, LOU Yongjiang1,*   

  1. 1. College of Food and Pharmaceutical Sciences, Ningbo University, Ningbo 315800, China; 2. College of Biological and Environmental Sciences, Zhejiang Wanli University, Ningbo 315100, China
  • Online:2019-05-15 Published:2019-05-28

摘要: 本研究以养殖大黄鱼鱼肉为原料,经过超高压处理(压力:150、200、250、300、350、400、450、500 MPa;保压时间:5、10、15、20、25、30 min)后,通过荧光分光光度法测定肌原纤维蛋白的内源荧光强度,采用傅里叶变换红外光谱法测定肌原纤维蛋白官能团结构,采用圆二色光谱法测定蛋白二级结构变化,采用激光拉曼光谱法分析蛋白质的化学基团信息,采用扫描电子显微镜法分析蛋白微观结构变化。结果表明:养殖大黄鱼鱼肉肌原纤维蛋白的荧光及最大发射波长受处理压力和保压时间的影响而变化,随着压力的增大和保压时间的延长,最大发射波长峰值变大;超高压处理影响了肌原纤维蛋白的三级结构,其氨基酸残基所处化学环境极性增强;超高压处理影响了肌原纤维蛋白的二级结构,其α-螺旋含量随压力的升高和保压时间的延长而逐渐降低;超高压处理影响蛋白构象变化并引起蛋白变性,压力越大、保压时间越长,其变性程度越大,变性程度直接影响着肌原纤维蛋白的微观结构。养殖大黄鱼肌原纤维蛋白在超高压处理后结构发生了变化,其二级、三级结构均有改变并引起蛋白变性,鱼肉品质随之发生变化。

关键词: 超高压, 养殖大黄鱼, 肌原纤维蛋白, 结构

Abstract: In this paper, large yellow croaker was subjected to ultra-high pressure treatment at pressures of 150, 200, 250, 300, 350, 400, 450 and 500 MPa for different durations of 5, 10, 15, 20, 25 and 30 min for modification of myofibrillar proteins. The endogenous fluorescence intensity of myofibrillar proteins was determined by fluorescence spectrophotometry, the myofibrillar protein functional structure was determined by Fourier transform infrared spectroscopy, and the secondary structure was determined by circular dichroism spectroscopy. Raman spectroscopy was employed to determine the information about chemical groups in the proteins, and the microstructure changes were observed by scanning electron microscopy. The results showed that the fluorescence intensity and maximum emission wavelength of myofibrillar proteins were influenced by pressure and holding time, and the maximum fluorescence emission intensity increased with the increase in the variables. Ultra-high pressure treatment affected the tertiary structure of myofibrillar proteins and enhanced the polarity of the surrounding environment of amino acid residues. Ultra-high pressure also affected the secondary structure; the content of α-helix structure gradually decreased with the increase in pressure and holding time. Moreover, ultra-high pressure affected protein conformational changes and caused protein denaturation; the degree of denaturation, directly affecting the microstructure of myofibrillar proteins, was positively correlated with pressure and holding time. Conclusively, the secondary and tertiary structure of myofibrillar proteins from cultured large yellow croaker was changed after ultra-high pressure treatment, causing protein denaturation and accordingly quality changes of fish meat.

Key words: high hydrostatic pressure, cultured large yellow croaker, myofibrillar protein, structure

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