氧化及不同离子强度下猪肉肌原纤维蛋白结合风味物质的研究

文章研究了猪肉肌原纤维蛋白氧化导致其结构功能发生改变及氧化和不同离子条件下其结合风味物质的能力变化。实验选择了2-甲基丁醛、3-甲基丁醛、己醛、辛醛、壬醛等5种风味物质，利用顶空结合气相色谱观察肌原纤维蛋白结合风味物质的能力。结果表明：经氧化的肌原纤维蛋白二级结构及功能发生了变化。氧化处理的肌原纤维蛋白对2-甲基丁醛和壬醛有促释放的作用，对3-甲基丁醛、己醛和辛醛的作用呈2,2-偶氮二(2-甲基丙基咪)二盐酸盐(AAPH)浓度依赖性。Na+的添加促进了氧化蛋白对己醛的释放，而Na⁺、K⁺、Ca²⁺和Mg²⁺的添加促进了氧化蛋白对2-甲基丁醛、3-甲基丁醛、辛醛和壬醛的吸收。因此，在肉及肉制品的加工贮藏过程，氧化易造成蛋白结构和功能的改变，进而影响蛋白质结合风味物质的能力；另外，氯化钠在肉制品中被其它盐部分替代造成蛋白质所处的离子环境发生改变，导致蛋白质结合风味物质的能力改变，从而使肉制品风味发生改变。

Effects of Oxidation and Different Ionic Environment on the Binding of Pork Myofibrillar Protein to Flavor Substances

The changes of structure and function of pork myofibrillar protein induced by oxidation and its ability to bind flavor substances under different ionic conditions were studied. 2-methyl-butanal, 3-methyl-butanal, hexanal, octanal and nonanal were selected as volatile compounds in the experiment. The ability of myofibrillar protein to bind volatile compounds was observed by headspace combined gas chromatography. The results confirmed that the secondary structure and function of oxidized myofibrillar protein changed. Oxidized myofibrillar protein could promote the release of 2-methyl-butanal and nonanal. Moreover, the effect of oxidized myofibrillar protein on 3-methyl-butanal, hexanal and octanal was dependent on AAPH concentration. The addition of Na+ promoted the release of hexanal, while the addition of Na+, K+, Ca2+ and Mg2+ promoted the absorption of 2-methyl-butanal, 3-methyl-butanal, octanal and nonal. Consequently, during the processing and storage of meat and meat products, oxidation of meat protein could change its structure and function, and then affect the ability of protein to combine flavor substances. In addition, sodium chloride is partially replaced by other salts in meat products, resulting in changes in the ionic environment of proteins, resulting in changes in the ability of proteins to combine flavor substances, thus changing the flavor of meat products.