Centro de Investigación en Alimentacion y Desarrollo A.C., Unidad Cuauhtémoc, Av. Rio Conchos S/N, Parque Industrial, Ciudad Cuauhtémoc, Chihuahua, México, C.P. 31570.
Facultad de Ciencias Químicas, Universidad Autónoma de Chihuahua, Circuito Universitario 8, Campus UACH II, Chihuahua, Chihuahua, México, C.P. 31125.
J Dairy Sci. 2022 Feb;105(2):981-989. doi: 10.3168/jds.2021-21071. Epub 2021 Nov 17.
Rennet milk curds were prepared under 4 different temperature and acidity conditions. The development of different types of inter-protein chemical bonds (disulfide, hydrophobic, electrostatic, hydrogen, and calcium bridges) was monitored for 60 min after curd cutting. Hydrophobic inter-protein interactions originally present in casein micelles in milk were substituted by electrostatic, hydrogen, and calcium bonds throughout the curd curing period. Disulfide bonds were not disturbed by the experimental conditions employed in the study, remaining at a constant level in all studied treatments. Acidification of curds increased the availability of soluble ionic calcium, increasing the relative proportion of calcium bridges at the expense of electrostatic-hydrogen bonds. Although pH defined the nature of the interactions established among proteins in curd, temperature modified the rate at which such bonds were formed.
凝乳在 4 种不同温度和酸度条件下制备。在切割凝乳后 60 分钟监测不同类型的蛋白质间化学键（二硫键、疏水键、静电键、氢键和钙桥）的形成情况。在凝乳固化过程中，牛奶中存在于酪蛋白胶束中的原始疏水蛋白质间相互作用被静电键、氢键和钙桥取代。二硫键不受研究中采用的实验条件的干扰，在所有研究处理中保持恒定水平。凝乳酸化增加了可溶性离子钙的可用性，增加了钙桥的相对比例，而减少了静电-氢键的比例。虽然 pH 值定义了凝乳中蛋白质之间建立的相互作用的性质，但温度改变了形成这些键的速度。
