食品科学 ›› 2022, Vol. 43 ›› Issue (8): 1-8.doi: 10.7506/spkx1002-6630-20210201-011

• 食品化学 •    

肌红蛋白血红素辅基氧化修饰对肌球蛋白功能特性及凝胶特性的影响

朱宏星,高田毅,黄杨,王鑫,葛庆丰,王道营,孙冲   

  1. (1.江苏省农业科学院农产品加工研究所,江苏 南京 210014;2.扬州大学食品科学与工程学院,江苏 扬州 225127)
  • 发布日期:2022-04-26
  • 基金资助:
    国家自然科学基金面上项目(31972137);江苏省食品质量安全重点实验室自主研究项目(2019JG001)

Effect of Oxidative Modification of Myoglobin Hemin Prosthetic Group on the Functional Properties and Gel Properties of Myosin

ZHU Hongxing, GAO Tianyi, HUANG Yang, WANG Xin, GE Qingfeng, WANG Daoying, SUN Chong   

  1. (1. Institute of Agri-products Processing, Jiangsu Academy of Agricultural Sciences, Nanjing 210014, China; 2. College of Food Science and Engineering, Yangzhou University, Yangzhou 225127, China)
  • Published:2022-04-26

摘要: 研究血红素辅基氧化修饰对肌球蛋白溶解度、粒径、乳化活性及乳化稳定性的影响,同时分析氧化修饰后肌球蛋白凝胶动态流变学特性、凝胶强度、保水性、水分分布变化、分子作用力以及微观结构变化,揭示氧化修饰对肌球蛋白凝胶保水性的影响机制。结果表明:低浓度血红素辅基处理肌球蛋白,蛋白溶解度无显著差异,乳化稳定性、热诱导凝胶的凝胶强度以及持水力有所提高,蛋白凝胶网络致密均匀,血红素辅基通过提高肌球蛋白凝胶分子间作用力(二硫键)使凝胶结构更加均匀有序、致密、孔洞尺寸小;同时提高了凝胶的表面亲水性和凝胶持水力,增强了凝胶中蛋白-水分子相互作用,进而增加了凝胶中不易流动水的比例,使更多水分保持在凝胶网络结构中。高浓度血红素辅基处理造成肌球蛋白溶解度降低、粒径增加、乳化活性及乳化稳定性降低同时凝胶网络结构被破坏、流变曲线趋于平坦,持水力降低。

关键词: 血红素辅基;肌球蛋白凝胶;蛋白氧化;保水性

Abstract: In this study, the impact of oxidative modification of hemin prosthetic group on the solubility, particle size, emulsifying activity and emulsion stability of myosin was investigated. Meanwhile, the changes in the dynamic rheological properties, gel strength, water-holding capacity, water distribution, intermolecular interaction forces and microstructure of heat-induced myosin gel were analyzed before and after the oxidative modification and the mechanism behind its effect on the water-holding capacity of heat-induced myosin gel was deciphered. The results showed that treatment with low concentrations of hemin prosthetic group had no impact on the solubility, but increased the emulsion stability, heat-induced gel strength and water-holding capacity of myosin, and made the gel network structure more uniform, ordered and compact with smaller holes in it by intermolecular interactions such as disulfide bonding. Besides, the treatment improved the surface hydrophilicity and water-holding capacity of the gel and enhanced the interaction between protein and water, consequently increasing the proportion of immobile water and retaining more water in the gel network structure. By contrast, high concentrations of hemin prosthetic group led to lower solubility, larger particle size, and worse emulsifying activity and emulsion stability of myosin, damaged the gel network structure, flattened the rheological curve, and weakened the water-holding capacity.

Key words: hemin prosthetic group; myosin gel; protein oxidation; water-holding capacity

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