Regester G O, Pearce R J, Lee V W, Mangino M E
Dairy Research Laboratory, CSIRO Division of Food Processing, Highett, Victoria, Australia.
J Dairy Res. 1992 Nov;59(4):527-32. doi: 10.1017/s0022029900027199.
Correlations were identified between levels of the native whey proteins, beta-lactoglobulin and alpha-lactalbumin and the surface and total hydrophobicities of cheese whey in response to different heat treatments. Heat-induced changes in the native beta-lactoglobulin content and surface hydrophobicity of whey exhibited the most significant linear relationship while correlations between total hydrophobicity and the native proteins were less significant because of an atypical rise in the n-heptane-binding capacity of whey after high-temperature treatment. The content of native beta-lactoglobulin in whey was more sensitive to heating than the content of native alpha-lactalbumin, while heat-related changes in the total hydrophobicity of whey were generally greater than similar changes in surface hydrophobicity.
研究发现，天然乳清蛋白（β-乳球蛋白和α-乳白蛋白）的水平与不同热处理条件下奶酪乳清的表面疏水性和总疏水性之间存在相关性。乳清中天然β-乳球蛋白含量和表面疏水性的热诱导变化呈现出最显著的线性关系，而总疏水性与天然蛋白质之间的相关性则不太显著，这是因为高温处理后乳清的正庚烷结合能力出现非典型上升。乳清中天然β-乳球蛋白的含量比天然α-乳白蛋白的含量对加热更敏感，而乳清总疏水性的热相关变化通常大于表面疏水性的类似变化。
