β-乳球蛋白纤维化过程中的界面及乳化性质

摘要

依据蛋白质在酸热环境下能通过自组装形成纤维状聚集体的特性,首先利用荧光强度、透射电子显微镜等手段对β-乳球蛋白纳米纤维的形成过程进行表征,再通过界面流变仪对各阶段产物的界面吸附及界面黏弹模量进行分析,并在此基础上对其乳化行为进行研究.结果表明:纤维化过程中不同阶段产物具有不同的界面及乳化行为.随着纤维化转变进行,混合体系的界面吸附能力以及界面黏弹模量逐渐增加.不同阶段产物能形成粒径在8.5～10.5 μm之间的稳定乳液,且乳化能力随着纤维化转变而增强,但过度纤维化转变不利于蛋白质的乳化稳定性.%When heated under acidic conditions,protein is self-assembled into fibrils.In this paper,the formation of β-lactoglobulin protein fibrils was characterized by fluorescence spectroscopy and transmission electron microscopy (TEM).Interfacial adsorption and interfacial viscoelasticity of the samples at different fibrillation stages were analyzed with an interfacial rheometer,and then their emulsifying behaviors were studied.Different interfacial and emulsifying properties of the dispersions from different fibrillation stages were observed.The interfacial adsorption ability and the viscoelasticity of the dispersions were increased as fibrillation progressed.Stable emulsions with average droplet size (D[3,2]) ranging from 8.5 to 10.5 μm could be formed from the fibrillation products at different stages,and the emulsifying capacity of the dispersions were shown to be increased with increasing degree of fibrillation.However,excessive fibrillation had a negative effect on the storage stability of the emulsions.