The effect of the addition of caseinomacropeptide (CMP) or desialylated CMP on the heat-induced denaturation and aggregation of whey proteins was investigated in the pH range 3 to 7 after heating at 80°C for 30 min. The rate and temperature of denaturation, the extent of aggregation, and the changes in secondary structure of the whey proteins heated in presence of CMP or desialylated CMP were measured. The sialic acid bound to CMP favored the denaturation and aggregation of whey proteins when the whey proteins were oppositely charged to CMP at pH 4. A transition occurred at pH 6, below which the removal of sialic acid enhanced the stabilizing properties of CMP against the denaturation and aggregation of the whey proteins. At pH >6, the interactions between desialylated CMP and the whey proteins led to more extensive denaturation and aggregation. Sialic acid bound to CMP influenced the denaturation and aggregation behavior of whey proteins in a pH-dependent manner, and this should be considered in future studies on the heat stability of such systems containing CMP.

中文翻译：

---

酪蛋白巨肽的去唾液酸化对乳清蛋白的变性和聚集的影响。

在80°C加热30分钟后，在3至7的pH范围内研究了酪蛋白巨肽（CMP）或去唾液酸化CMP对热诱导的乳清蛋白变性和聚集的影响。测量了在CMP或脱唾液酸化CMP存在下加热的乳清蛋白的变性速率和温度，聚集程度以及二级结构的变化。当乳清蛋白在pH 4处相反地带入CMP时，与CMP结合的唾液酸有利于乳清蛋白的变性和聚集。在pH 6时发生过渡，在该跃迁以下，唾液酸的去除增强了CMP抗变性的稳定性。和乳清蛋白的聚集。在pH> 6时，去唾液酸化CMP和乳清蛋白之间的相互作用导致更广泛的变性和聚集。