Linear and nonlinear interface rheological behaviors and structural properties of pea protein (vicilin, legumin, albumin)
Linear and nonlinear interface rheological behaviors and structural properties of pea protein (vicilin, legumin, albumin)
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DOI：
10.1016/j.foodhyd.2023.108500
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发表时间：
2023-02
影响因子：
10.7
通讯作者：
Qian Shen;Jing Li;Xiao Shen;Xinyu Zhu;Jun Dai;Cuie Tang;R. Song;Bin Li;Yijie Chen
中科院分区：
文献类型：
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作者：
Qian Shen;Jing Li;Xiao Shen;Xinyu Zhu;Jun Dai;Cuie Tang;R. Song;Bin Li;Yijie Chen
在这项研究中，PPI及其主要组分蛋白质的结构特性进行了研究。豌豆球蛋白（7S）具有更灵活的结构，而豆球蛋白（11 S）具有更高的疏水性。白蛋白（2S）结构简单、松散，界面容量较弱。蛋白质结构的差异导致了相应的蛋白质稳定界面系统。为了揭示蛋白质结构与界面流变特性之间的联系，采用线性和非线性流变行为分析了蛋白质与蛋白质界面的微观结构。Lissajous图表明，7S蛋白在拉伸过程中可形成应变软化的界面。同时，11 S倾向于形成具有应变硬化的刚性界面层。蛋白质结构中的疏水基团促进了界面网络结构的形成，从而改善了乳化稳定性。相比之下，2S稳定的油水界面的微观结构容易被破坏，这与其较低的乳化活性相一致。蛋白质在油水界面上吸附行为的结构-界面性质可以反映界面上的结构重排，预测界面微观结构。本研究揭示了蛋白质稳定乳剂的稳定性与蛋白质结构的关系。
In the study, the structural properties of PPI and its major component proteins were investigated. The vicilin (7S) showed a more flexible structure, while the legumin (11S) possessed higher hydrophobicity. The albumin (2S) with simple and loose structure presented the weaker interfacial capacity. The difference in the protein structure was responsible for the corresponding protein stabilized interface system. In order to reveal the connection between protein structure and interface rheological properties, the linear and nonlinear rheological behaviors of the formed interface were used to analyze the interfacial microstructure. The results of Lissajous plots showed the proteins of 7S could form an interface with a strain softening behavior in extension. Meanwhile, the 11S tended to form a rigid interfacial layer with the strain hardening. The hydrophobic groups within the protein structure facilitated the formation of the interfacial network structure, leading to an improved emulsifying stability. In contrast, the microstructure of the oil-water interface stabilized by 2S was easy to break, which was consistent with its lower emulsifying activity. The structure-interface properties of the protein adsorption behavior at the oil-water interface could reflect the structural rearrangement at the interface and predict the interfacial microstructure. This research showed the relationship between the stability of protein stabilized emulsion and the protein structure.