以未经热处理的水牛乳酪蛋白为对照，探究常见的4种热杀菌处理条件对水牛乳酪蛋白结构的影响，结果表明，加热产生大分子聚合物，大分子聚合物主要由二硫键联接形成；80 ℃时，水牛乳酪蛋白的起泡性和起泡稳定性最高，起泡性为137.33%，起泡稳定性为32.33%；超高温灭菌（135 ℃）条件下，水牛乳酪蛋白的平均粒径显著增加，粒径为516.2 nm；超高温灭菌乳的酪蛋白胶束被破坏，表面结构发生变化；热处理造成酪蛋白的二级结构发生变化，135 ℃条件下，α-螺旋结构和β-折叠含量显著下降，最小分别为13.76%和35.84%；酪蛋白的三级结构和表面疏水性发生改变，其中巴氏杀菌乳（80 ℃），荧光强度最高为582.44，超高温灭菌乳表面疏水性最大为258.96。基于上述结果，说明巴氏杀菌条件对酪蛋白的影响比较小，超高温条件容易造成蛋白聚集，从而影响产品的稳定性，80 ℃是较佳的热杀菌处理条件。从而为提升生产过程中水牛乳制品的稳定性提供理论基础。

The non-heat-treated buffalo milk casein was used as a control to investigate the effects of four common heat treatments on the structure of buffalo milk casein. The results showed that macromolecular polymers were produced by heating and were mainly formed by proteins linked by disulfide bonds. After the heat treatment of 80 ℃, buffalo milk casein had the highest foaming capacity (FC) and foaming stability (FS) at 137.33% and 32.33%, respectively. After ultra-high temperature sterilization (135 ℃), the buffalo milk casein enlarged significantly to 516.2 nm, with destroyed casein micelles and an altered surface structure. Heat treatments modified the secondary structure of casein; notably, at 135 ℃, the α-helix and β-sheet contents decreased significantly, with minimum values of 13.76% and 35.84%, respectively. Heat treatments also altered the tertiary structure and surface hydrophobicity of casein; the pasteurized milk (80 ℃) had the highest fluorescence intensity at 582.44, and the ultrahigh-temperature sterilized milk had the highest surface hydrophobicity at 258.96. These results indicated that pasteurization has a relatively small effect on casein, while the ultra-high temperature condition tends to cause protein aggregation, affecting product stability. Therefore, 80 ℃ is an optimal temperature for the heat treatment of buffalo milk. The findings of this study provide a theoretical basis for improving the stability of buffalo dairy products in the production process.

国家重点研发计划项目（2022YFD1600102）；广西科技基地和人才专项（桂科AD21220004）；国家现代农业产业技术体系广西创新团队（nycytxgxcxtd-2021-21-02）；南宁市创新创业领军人才“邕江计划”（2021018）