相对于牛乳而言,羊乳脂肪球膜蛋白的热稳定性较差，从而影响其一部分功能特性并限制了羊乳的应用。基于前期研究结果，我们推测羊乳脂肪球膜蛋白热稳定差的主要诱因是由于其膜蛋白糖基化修饰程度较低从而导致脂肪球膜蛋白间较易发生热聚集。因此，本研究旨在首先验证蛋白糖基化修饰对乳脂肪球膜蛋白热稳定性的影响及其机制；同时，运用糖蛋白质组学的手段表征不同糖基化程度的内源性和外源性糖基化修饰的羊乳脂肪球膜蛋白模型，揭示不同糖基化程度对脂肪球膜蛋白间聚集的影响机制；最后，建立不同糖链和不同糖基化位点的模型，阐明糖基化影响羊乳脂肪球膜蛋白聚集的主要因素。本研究结果将有助于为提高脂球膜蛋白热稳定性提供理论支撑。

Goat milk fat globule membrane (MFGM) proteins has lower thermo stability in comparison with bovine MFGM proteins. The lower thermo stability induced functionality loss is the key points impacting the application of goat milk in the dairy processing. Based on the previous results, we propose a hypothesis that the lower thermo stability of goat MFGM proteins is related to protein aggregation. Therefore, our aim is to confirm the effect of glycosylation/glycation on the thermo stability of goat milk MFGM proteins. Furthermore, applying glycomics techniques to show the differences in the glycosylation/glycation extend through identify and quantify glycosylated /glycated proteins, oligosaccharides, and their locations in goat MFGM proteins models with different lactation and different glucose incubation time. In addition, to evaluate how the type of oligosaccharides and their locations influence the protein aggregation of goat MFGM proteins during thermo treatment through different goat MFGM protein models. The accomplishment of this study will be expected to provide guidance on the improvement of thermo induced denaturation of goat MFGM proteins and keeping the most of their functionality.