牛心氧合肌红蛋白的分离纯化及氧化稳定性研究  

Isolation, Characterization and Redox Stability of Oxymyoglobin from Bovine Heart

作　　者：陈景宜[1] 牛力[1] 黄明[1] 周光宏[1] 

机构地区：[1]南京农业大学食品科技学院,教育部肉品加工与质量控制重点实验室,江苏南京210095

出　　处：《食品科学》2013年第13期1-5,共5页Food Science

基　　金：国家自然科学基金项目(30972133);国家公益性行业科研专项(201303083-2);苏北科研专项(201060090)

摘　　要：为了探讨牛心中氧合肌红蛋白的氧化稳定特性,利用硫酸铵分级沉淀(75%～100%)和Sephadex G-75层析柱分离纯化得到纯的肌红蛋白,并经分光光度扫描光谱鉴定。研究在不同的温度(20～60℃)、pH值(3.0～11.0)条件下氧合肌红蛋白的稳定性,并将氧合肌红蛋白分别与4-羟基壬烯醛(HNE)、乳酸一起孵育,测定HNE和乳酸对肌红蛋白氧化还原稳定性的影响。结果表明:随着温度的升高,氧合肌红蛋白稳定性减弱,高铁肌红蛋白生成量增大。氧合肌红蛋白在pH7.0时的稳定性最高,在pH3.0时失去了其特征吸收峰。与对照组相比,HNE促进了高铁肌红蛋白的形成,而乳酸则降低了高铁肌红蛋白的含量。氧合肌红蛋白在中性及偏碱性的环境中氧化还原稳定性显著高于酸性环境(P<0.01),HNE能促进氧合肌红蛋白的自动氧化,而乳酸能抑制氧合肌红蛋白的自动氧化。This study aimed to characterize the redox stability of oxymyoglobin from bovine heart.Myoglobin was isolated by ammonium sulphate precipitation（75%—100% saturation）,followed by Sephadex G-75 chromatography.Its purity was identified by scanning spectrophotometry.The pH and thermal stability of oxymyoglobin were tested over a pH range of 3.0—11.0 and a temperature range of 20—60 ℃.In addition,oxymyoglobin was incubated with 4-hydroxy-2-nonenal（HNE） and lactic acid,the redox stability of myoglobin was expressed by metmyoglobin percentage.The results showed that the stability of oxymyoglobin was decreased and the formation of metmyoglobin increased with increasing temperature.Metmyoglobin had the highest stability at pH 7.0,where the characteristic absorption peak of myoglobin disappeared.When compared with the control group,HNE improved the accumulation of metmyoglobin,while lactic acid decreased the accumulation of metmyoglobin.Myoglobin redox stability in neutral and alkaline environment was significantly higher than that in acid environment（P 0.01）.Moreover,HNE improved the autoxidation of oxymoglobin,while lactate inhibited the autoxidation of oxymoglobin.

关 键 词：氧合肌红蛋白 高铁肌红蛋白 氧化还原稳定性 热稳定性 

分 类 号：TS251.1[轻工技术与工程—农产品加工及贮藏工程]