2023, 43(2): 95-103. doi: 10.3969/j.issn.1673-9159.2023.02.012
关键词： 肌球蛋白 , pH值 , 乳液 , 乳化稳定性 , 界面蛋白
Keywords： myosin , pH value , emulsion , emulsion stability , interfacial protein
【目的】探讨pH值对肌球蛋白乳化稳定性及界面蛋白组成和结构的影响。【方法】设定2.0、5.0、7.0、11.0等4种pH值，通过pH偏移法探究其对罗非鱼（Oreochromis niloticus）肌球蛋白乳化性的影响，采用高压均质法制备罗非鱼肌球蛋白-大豆油乳液，分析不同pH值条件下罗非鱼肌球蛋白乳液的稳定性、界面蛋白组成及分子结构的变化。【结果】pH为5.0时，肌球蛋白的乳化性最差，乳液粒径最大（P < 0.05），Zeta-电位绝对值最小（P < 0.05），界面蛋白α-螺旋含量最低，无规则卷曲含量最多，乳液在贮藏期内明显分层。调节pH值至2.0、7.0和11.0时，肌球蛋白的乳化活性与乳化稳定性增强，乳液贮藏7 d未分层。电泳结果显示，乳液体系中界面蛋白主要由肌球蛋白重链组成，pH 2.0和5.0时蛋白在界面发生交联聚集，而pH 7.0和11.0时蛋白在界面聚集少，与未经处理的肌球蛋白相比，乳液及界面吸附状态肌球蛋白的二级结构发生明显变化，α-螺旋含量减少（P<0.05）。比较而言，pH 11.0条件下，肌球蛋白乳液粒径最小（P < 0.05），界面蛋白分子结构部分展开，与油滴相互作用增强，肌球蛋白的乳化性最好。【结论】pH值的变化能诱导肌球蛋白分子结构及界面特性的改变，从而改善肌球蛋白的乳化性能。
【目的】探讨pH值对肌球蛋白乳化稳定性及界面蛋白组成和结构的影响。【方法】设定2.0、5.0、7.0、11.0等4种pH值，通过pH偏移法探究其对罗非鱼（Oreochromis niloticus）肌球蛋白乳化性的影响，采用高压均质法制备罗非鱼肌球蛋白-大豆油乳液，分析不同pH值条件下罗非鱼肌球蛋白乳液的稳定性、界面蛋白组成及分子结构的变化。【结果】pH为5.0时，肌球蛋白的乳化性最差，乳液粒径最大（P < 0.05），Zeta-电位绝对值最小（P < 0.05），界面蛋白α-螺旋含量最低，无规则卷曲含量最多，乳液在贮藏期内明显分层。调节pH值至2.0、7.0和11.0时，肌球蛋白的乳化活性与乳化稳定性增强，乳液贮藏7 d未分层。电泳结果显示，乳液体系中界面蛋白主要由肌球蛋白重链组成，pH 2.0和5.0时蛋白在界面发生交联聚集，而pH 7.0和11.0时蛋白在界面聚集少，与未经处理的肌球蛋白相比，乳液及界面吸附状态肌球蛋白的二级结构发生明显变化，α-螺旋含量减少（P<0.05）。比较而言，pH 11.0条件下，肌球蛋白乳液粒径最小（P < 0.05），界面蛋白分子结构部分展开，与油滴相互作用增强，肌球蛋白的乳化性最好。【结论】pH值的变化能诱导肌球蛋白分子结构及界面特性的改变，从而改善肌球蛋白的乳化性能。
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