蛋白氧化对肌原纤维蛋白凝胶构效关系的影响  

Effect of Protein Oxidation on the Structure-Activity Relationship of Myofibrillar Protein Gels

作　　者：赵冰 李素 张顺亮 周慧敏 潘晓倩 任双 李家鹏 陈文华 赵燕 王守伟 

机构地区：[1]北京食品科学研究院,中国肉类食品综合研究中心,肉类加工技术北京市重点实验室,北京100068

出　　处：《食品科学》2018年第3期55-61,共7页Food Science

基　　金：“十二五”国家科技支撑计划项目(2015BAD28B01); 北京市自然科学基金(青年项目)(6164035); 公益性行业(农业)科研专项(201303082)

摘　　要：研究不同浓度H_2O_2氧化体系中肌原纤维蛋白的氧化情况及氧化程度对其凝胶特性的影响,并测定了肌原纤维蛋白凝胶二级结构和空间结构的变化。结果表明:H_2O_2形成的羟自由基可以促进肌原纤维蛋白的氧化,蛋白质的氧化程度随着H_2O_2浓度的升高而增加;肌原纤维蛋白的凝胶特性随着蛋白氧化程度的增加而发生规律性的变化,蛋白凝胶强度、凝胶保水性、储能模量和损失模量随着H_2O_2浓度的升高而降低,表面疏水性呈现出增加的趋势;随着H_2O_2浓度的升高,结构稳定的α-螺旋和β-折叠部分遭到破坏,蛋白质由稳定的结构向不稳定转变;通过扫描电子显微镜观察蛋白凝胶的网状结构,表明蛋白氧化阻碍了蛋白质稳定凝胶空间结构的形成。The effects of different concentrations of H2O2 on the degree of oxidation and gelation properties of myofibrillar proteins were studied, and we also examined changes in the secondary structure and spatial structure of myofibrillar protein gels after H2O2 oxidation. The results showed that hydroxyl radicals derived from H2O2 could promote the oxidation of myofibrillar proteins, and that the degree of oxidation increased with increasing H2O2 concentration. The gelation properties of myofibrillar proteins regularly changed with the degree of oxidation. The gel strength, water retention, storage modulus and loss modulus decreased, whereas the surface hydrophobicity showed an increasing trend. Furthermore, the secondary structures of α-helix and β-sheet were partially destroyed and became unstable as H2O2 concentration increased. By observing the network structure of the protein gels by scanning electron microscopy, it was confirmed that protein oxidation hindered protein gels from forming a spatial structure.

关 键 词：肌原纤维蛋白 蛋白氧化 凝胶特性 二级结构 空间结构 

分 类 号：TS251.1[轻工技术与工程—农产品加工及贮藏工程]