Yan Daomin, Zhang Lina, Zhu Yixuan, Han Mengyu, Wang Yancong, Tang Jun, Zhou Peng
State Key Laboratory of Food Science & Technology, Jiangnan University, Wuxi 214122, China.
Foods. 2022 Sep 5;11(17):2705. doi: 10.3390/foods11172705.
Milk proteins are prone to changes during the heat treatment process. Here, we aimed to study the changes in caprine milk fat globule membrane (MFGM) proteins with three heat treatment processes-ultra-pasteurization (85 °C, 30 min), ultra-high-temperature instant sterilization (135 °C, 5 s), and spray-drying (inlet, 160 °C and outlet, 80 °C)-using the label-free proteomics technique. A total of 1015, 637, 508, and 738 proteins were identified in the raw milk, ultra-pasteurized milk, ultra-high-temperature instant sterilized milk, and spray-dried reconstituted milk by using label-free proteomics techniques, respectively. Heat treatment resulted in a significant decrease in the relative intensity of MFGM proteins, such as xanthine dehydrogenase/oxidase, butyrophilin subfamily 1 member A, stomatin, and SEA domain-containing protein, which mainly come from the membrane, while the proteins in skimmed milk, such as β-lactoglobulin, casein, and osteopontin, increased in MFGM after heat treatment. Among these different heat treatment groups, the procedure of spray-drying resulted in the least abundance reduction of caprine milk MFGM proteins. Additionally, it showed heating is the key process affecting the stability of caprine MFGM protein rather than the spray-drying process. These findings provide new insights into the effects of heat treatment on caprine MFGM protein composition and potential biological functions.
乳蛋白在热处理过程中容易发生变化。在此，我们旨在使用无标记蛋白质组学技术研究三种热处理工艺——超高温瞬时灭菌（85°C，30分钟）、超高温瞬时灭菌（135°C，5秒）和喷雾干燥（进料口160°C，出料口80°C）——对山羊乳脂肪球膜（MFGM）蛋白的影响。通过无标记蛋白质组学技术，分别在原料乳、超高温瞬时灭菌乳、超高温瞬时灭菌乳和喷雾干燥复原乳中鉴定出1015、637、508和738种蛋白质。热处理导致主要来自膜的MFGM蛋白（如黄嘌呤脱氢酶/氧化酶、嗜乳脂蛋白亚家族1成员A、血影蛋白和含SEA结构域的蛋白）相对强度显著降低，而热处理后脱脂乳中的蛋白（如β-乳球蛋白、酪蛋白和骨桥蛋白）在MFGM中的含量增加。在这些不同的热处理组中，喷雾干燥过程导致山羊乳MFGM蛋白丰度降低最少。此外，结果表明加热是影响山羊MFGM蛋白稳定性的关键过程，而非喷雾干燥过程。这些发现为热处理对山羊MFGM蛋白组成和潜在生物学功能的影响提供了新的见解。
