食品科学 ›› 2019, Vol. 40 ›› Issue (13): 81-86.doi: 10.7506/spkx1002-6630-20180518-265

• 食品工程 • 上一篇    下一篇

电子束辐照对鲈鱼肉肌原纤维蛋白生化特性及其构象的影响

张 晗,高 星,宣仕芬,徐大伦,张进杰,钱云霞,杨文鸽   

  1. 宁波大学食品与药学学院,浙江省动物蛋白食品精深加工重点实验室,浙江 宁波 315211
  • 出版日期:2019-07-15 发布日期:2019-07-23
  • 基金资助:
    国家自然科学基金面上项目(31371793);宁波大学研究生科研创新基金资助项目(G18112)

Effect of Electron Beam Irradiation on Biochemical Properties and Structure of Myofibrillar Protein from Lateolabrax japonicus Meat

ZHANG Han, GAO Xing, XUAN Shifen, XU Dalun, ZHANG Jinjie, QIAN Yunxia, YANG Wenge   

  1. Key Laboratory of Animal Protein Food Deep Processing Technology of Zhejiang Province, College of Food and Pharmaceutical Sciences, Ningbo University, Ningbo 315211, China
  • Online:2019-07-15 Published:2019-07-23

摘要: 为研究电子束辐照在水产品保鲜应用上的可行性,采用1、3、5、7 kGy剂量电子束辐照处理鲈鱼肉,以盐溶蛋白含量、巯基含量、二硫键含量、Ca2+-ATPase活力、表面疏水性、羰基含量及其构象单元组成等为指标,探究不同剂量辐照对鲈鱼肉肌原纤维蛋白生化特性及其空间结构的影响。与对照组相比,1 kGy辐照组除总巯基含量显著上升外(P<0.05),其他指标水平均无显著变化(P>0.05)。随着辐照剂量继续上升,盐溶蛋白含量、活性巯基含量、Ca2+-ATPase活力下降,羰基和二硫键含量上升,且呈剂量-效应关系;表面疏水性则随辐照剂量上升先增大后减小,并于5 kGy时达到最大值。圆二色光谱分析结果显示,随着辐照剂量的上升,鲈鱼肉肌原纤维蛋白中的α-螺旋结构向β-折叠转化。结果显示高剂量辐照会引起鲈鱼肉肌原纤维蛋白氧化,利用电子束辐照保鲜鲈鱼肉应控制剂量,实验结果为辐照保鲜鱼肉提供了依据。

关键词: 电子束辐照, 鲈鱼, 肌原纤维蛋白, 生化特性, 圆二色光谱

Abstract: To study the feasibility of electron beam irradiation for application to aquatic products, the effects of different electron beam irradiation doses (1, 3, 5 and 7 kGy) on the biochemical properties and structure of myofibrillar protein from Lateolabrax japonicus meat such as salt-soluble protein content, sulfhydryl content, disulfide bond content, Ca2+-ATPase activity, surface hydrophobicity, carbonyl content and conformation. The results showed that total sulfhydryl content was significantly higher in the 1 kGy group compared to the control group (P < 0.05), while there was no significant change in any other indices (P > 0.05). As the irradiation dose continued to increase, the contents of salt-soluble protein content and reactive sulfhydryl and ATPase activity decreased significantly whereas carbonyl and disulfide bond contents increased; higher irradiation dose resulted in more significant changes. The surface hydrophobicity of myofibrillar protein rose with irradiation dose up to 5 kGy and then decreased at higher doses. Circular dichroism (CD) spectroscopic analysis indicated that the conformation of myofibrillar protein was converted from an α-helix to β-sheet structure as a result of increasing irradiation dose. Higher doses of electron beam irradiation could cause the oxidation of myofibrillar protein. To minimize the effect on myofibrillar protein, L. japonicus meat should be irradiated at low doses before cold storage. These results provide the basis for the application of electron beam irradiation in the preservation of fish meat.

Key words: electron beam irradiation, Lateolabrax japonicus, myofibrillar protein, biochemical properties, circular dichroism spectroscopy

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