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β-伴大豆球蛋白和大豆球蛋白修饰的脂质体:构建、结构和体外消化稳定性。

Liposomes decorated with β-conglycinin and glycinin: Construction, structure and in vitro digestive stability.

机构信息

College of Food Science, Northeast Agricultural University, Harbin, Heilongjiang 150030, China.

College of Food Science and Engineering, Hainan University, Haikou, Hainan 570228, China.

出版信息

Int J Biol Macromol. 2024 Jun;269(Pt 1):131900. doi: 10.1016/j.ijbiomac.2024.131900. Epub 2024 Apr 26.

Abstract

Liposomes were modified with different proportions of β-conglycinin (7S) and glycinin (11S) to form Lip-7S and Lip-11S. The morphology, interaction and in vitro simulated digestion of liposomes were studied. The particle size of Lip-7S was smaller than that of Lip-11S. When the values of Lip-7S and Lip-11S were 1:1 and 1:0.75, respectively, the ζ-potential had the maximum absolute value and the dispersion of the system was good. The results of multispectral analysis showed that hydrogen-bond and hydrophobic interaction dominated protein-modified liposomes, the protein structure adsorbed on the surface of liposomes changed, the content of α-helix decreased, and the structure of protein-modified liposomes became denser. The surface hydrophobicity and micropolarity of liposomes decreased with the increase of protein ratio, and tended to be stable after Lip-7S (1:1) and Lip-11S (1:0.75). Differential scanning calorimetry showed that Lip-7S had higher phase transition temperature (≥170.5 °C) and better rigid structure. During simulated digestion, Lip-7S (22.5 %) released less Morin than Lip (40.6 %) and Lip-11S (26.2 %), and effectively delayed the release of FFAs. The environmental stability of liposomes was effectively improved by protein modification, and 7S had better modification effect than 11S. This provides a theoretical basis for 7S and 11S modified liposomes, and also provides a data reference for searching for new materials for stabilization of liposomes.

摘要

采用不同比例的β-伴大豆球蛋白(7S)和大豆球蛋白(11S)对脂质体进行修饰,分别形成 Lip-7S 和 Lip-11S。研究了脂质体的形态、相互作用和体外模拟消化。Lip-7S 的粒径小于 Lip-11S。当 Lip-7S 和 Lip-11S 的值分别为 1:1 和 1:0.75 时,ζ-电位具有最大绝对值,且体系分散性良好。多光谱分析结果表明,氢键和疏水相互作用主导蛋白质修饰脂质体,蛋白质结构吸附在脂质体表面发生变化,α-螺旋含量减少,蛋白质修饰脂质体结构变得更加致密。随着蛋白质比例的增加,脂质体的表面疏水性和微极性降低,在 Lip-7S(1:1)和 Lip-11S(1:0.75)之后趋于稳定。差示扫描量热法表明 Lip-7S 具有较高的相变温度(≥170.5°C)和更好的刚性结构。在模拟消化过程中,Lip-7S(22.5%)释放的莫林比 Lip(40.6%)和 Lip-11S(26.2%)少,且能有效延迟 FFA 的释放。蛋白质修饰有效提高了脂质体的环境稳定性,7S 的修饰效果优于 11S。这为 7S 和 11S 修饰的脂质体提供了理论依据,也为寻找稳定脂质体的新材料提供了数据参考。

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