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通过多尺度方法探索γ-谷维素对α-乳白蛋白或β-乳球蛋白负载的 Pickering 乳液凝胶稳定机制的作用。

Exploring the role of γ-Oryzanol on stabilization mechanism of Pickering emulsion gels loaded by α-Lactalbumin or β-Lactoglobulin via multiscale approaches.

机构信息

Key Laboratory of Dairy Science (Northeast Agricultural University), Ministry of Education, College of Food Science, Northeast Agricultural University, Harbin, 150030, PR China; College of Food Science and Engineering, Engineering Technology Research Center for Processing and Comprehensive Utilization of Idesia polycarpa of National Forestry and Grassland Administration, Guiyang University, Guiyang 550005, PR China; Heilongjiang Green Food Science Research Institute, Harbin 150028, PR China.

Key Laboratory of Dairy Science (Northeast Agricultural University), Ministry of Education, College of Food Science, Northeast Agricultural University, Harbin, 150030, PR China.

出版信息

Food Chem. 2024 Nov 1;457:140096. doi: 10.1016/j.foodchem.2024.140096. Epub 2024 Jun 14.

DOI:10.1016/j.foodchem.2024.140096
PMID:38905830
Abstract

The research explored the role of γ-oryzanol (γs) on stabilization behavior of Pickering emulsion gels (PEGs) loaded by α-lactalbumin (α-LA) or β-lactoglobulin (β-LG), being analyzed by experimental and computer methods (molecular dynamic simulation, MD). Primarily, the average particle size of β-LG-γS was expressed 100.07% decrease over that of α-LA-γS. In addition, γs decreased the dynamic interfacial tension of two proteins with the order of β-LG < α-LA. Meanwhile, quartz crystal microbalance with dissipation proved that β-LG-γS exhibited higher adsorption mass and denser rigid interface layer than α-LA-γS. Moreover, the hydrophobic group of γS had electrostatic repulsion with polar water molecules in the aqueous phase, which spread to the oil phase. β-LG-γS had lower RMSD/Rg value and narrower fluctuation compared with α-LA-γS. This work strength the exploration of interfacial stabilization mechanism of whey protein-based PEGs, which enriched its theoretical research for industrial-scale production as the replacement of trans fat and cholesterol.

摘要

本研究通过实验和计算机方法(分子动力学模拟,MD)探讨了γ-谷维素(γs)对载有α-乳白蛋白(α-LA)或β-乳球蛋白(β-LG)的 Pickering 乳液凝胶(PEGs)稳定行为的作用。首先,β-LG-γS 的平均粒径表示比α-LA-γS 减少了 100.07%。此外,γs 降低了两种蛋白质的动态界面张力,顺序为β-LG<α-LA。同时,石英晶体微天平耗散证明,β-LG-γS 的吸附质量更高,刚性界面层更致密。此外,γs 的疏油基团与水相中极性水分子具有静电排斥作用,这种排斥作用会扩散到油相。与α-LA-γS 相比,β-LG-γS 的 RMSD/Rg 值更低,波动范围更窄。这项工作加强了对乳清蛋白基 PEGs 界面稳定机制的探索,为其在工业规模生产中替代反式脂肪和胆固醇的理论研究提供了更多的支持。

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