Air-water interfacial properties and quantitative description of pea protein isolate-Tween 20
Air-water interfacial properties and quantitative description of pea protein isolate-Tween 20
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DOI：
10.1016/j.foodhyd.2023.108568
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发表时间：
2023-02
影响因子：
10.7
通讯作者：
Qian Shen;Wei-Bin Zheng;Fei Han;Jingnan Zuo;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;Wei-Bin Zheng;Fei Han;Jingnan Zuo;Jun Dai;Cuie Tang;R. Song;Bin Li;Yijie Chen
研究了豌豆分离蛋白（PPI）和吐温20（T20）的气-水界面性质。动态泡沫分析仪结果表明，0.5%PPI-0.1%T20体系制备的泡沫在30 min时具有较高的泡沫稳定性，且气泡尺寸分布均匀。利用原子力显微镜（AFM）对LB膜进行成像，观察了吐温20在空气-水界面上对蛋白质的置换作用。非离子表面活性剂Tween 20置换豌豆分离蛋白时，表面压力增大，复合物表面弹性模量减小。基于LB膜的AFM观察，定量分析表明泡沫网络中的蛋白质量增加。泡沫稳定性的提高与泡沫平台边缘蛋白质网络的形成有关。AFM结果表明，T20可以取代空气-水界面上的蛋白质，但与PPI稳定的泡沫相比，0.1%T20的加入可以增加豌豆蛋白的相对含量，从而导致泡沫膜上蛋白质网络的增加，从而提高泡沫的稳定性。该研究有助于加深对吐温20在气-水界面置换蛋白质的认识，从而改善蛋白质-表面活性剂稳定的泡沫基食品的品质。
The air-water interfacial properties of pea protein isolate (PPI) and Tween 20 (T20) were investigated in this study. The result of dynamic foam analyzer showed that the foam prepared by 0.5%PPI-0.1%T20 exhibited higher foam stability at 30 min and uniform bubble size distribution. The protein displacement by Tween 20 at the air-water interface was observed by atomic force microscopy (AFM) through the imaging of Langmuir-Blodgett (LB) films. During the displacement of pea protein isolate by the nonionic surfactant Tween 20, the surface pressure was increased while the complex surface dilatational modulus was decreased. Based on the AFM observations of the LB films, the quantitative analysis indicated the increased protein quantity in the foam network. To be emphasized, the formation of protein network at the plateau border of foams contributed to the increased foam stability. The AFM results showed that the protein at the air-water interface could be replaced by T20, but comparing with the PPI-stabilized foam, the addition of 0.1% T20 could increase the relative quantity of vicilin, thus leading to the increase of interconnected protein network at foam film to improve the foam stability. The research could promote the understanding of protein displacement by Tween 20 at the air-water interface, which could improve the quality of protein-surfactant stabilized foam-based foods.