Unidad de Ciencia y Tecnología de Lácteos, Instituto Tecnológico Suroeste, Universidad Tecnológica del Uruguay, La Paz, Colonia Piamontesa, Colonia, 70200, Uruguay.
Department of Food Science, Pennsylvania State University, University Park 16802.
J Dairy Sci. 2022 Sep;105(9):7230-7241. doi: 10.3168/jds.2021-21738. Epub 2022 Jul 22.
Ionic conditions affect the denaturation and gelling of whey proteins, affecting the physical properties of foods in which proteins are used as ingredients. We comprehensively investigated the effect of the presence of commonly used emulsifying salts on the denaturation and gelling properties of concentrated solutions of β-lactoglobulin (β-LG) and whey protein isolate (WPI). The denaturation temperature in water was 73.5°C [coefficient of variation (CV) 0.49%], 71.8°C (CV 0.38%), and 69.9°C (CV 0.41%) for β-LG (14% wt/wt), β-LG (30% wt/wt), and WPI (30% wt/wt), respectively. Increasing the concentration of salts, except for sodium hexametaphosphate, resulted in a linear increase in the denaturation temperature of WPI (kosmotropic behavior) and an acceleration in its gelling rate. Sodium chloride and tartrate salts exhibited the strongest effect in protecting WPI against thermal denaturation. Despite the constant initial pH of all solutions, salts having buffering capacity (e.g., phosphate and citrate salts) prevented a decrease in pH as the temperature increased above 70°C, resulting in a decline in denaturation temperature at low salt concentrations (≤0.2 mol/g). When pH was kept constant at denaturation temperature, all salts except sodium hexametaphosphate, which exhibited chaotropic behavior, exhibited similar effects on denaturation temperature. At low salt concentration, gelation was the controlling step, occurring up to 10°C above denaturation temperature. At high salt concentration (>3% wt/wt), thermal denaturation was the controlling step, with gelation occurring immediately after. These results indicate that the ionic and buffering properties of salts added to milk will determine the native versus denatured state and gelation of whey proteins in systems subjected to high temperature, short time processing (72°C for 15 s).
离子条件会影响乳清蛋白的变性和胶凝,从而影响蛋白质作为成分的食品的物理性质。我们全面研究了常用乳化盐的存在对浓缩β-乳球蛋白(β-LG)和乳清蛋白分离物(WPI)溶液变性和胶凝特性的影响。在水中,β-LG(14%wt/wt)、β-LG(30%wt/wt)和 WPI(30%wt/wt)的变性温度分别为 73.5°C[变异系数(CV)0.49%]、71.8°C(CV 0.38%)和 69.9°C(CV 0.41%)。除了六偏磷酸钠外,增加盐的浓度会导致 WPI 的变性温度线性升高(正渗透行为),并加速其胶凝速率。氯化钠和酒石酸盐对 WPI 热变性的保护作用最强。尽管所有溶液的初始 pH 保持不变,但具有缓冲能力的盐(如磷酸盐和柠檬酸盐)可防止 pH 在温度升高超过 70°C 时下降,从而导致低盐浓度(≤0.2mol/g)下变性温度下降。当 pH 在变性温度下保持恒定时,除了表现出反渗透行为的六偏磷酸钠外,所有盐对变性温度的影响相似。在低盐浓度下,胶凝是控制步骤,发生在变性温度以上 10°C。在高盐浓度(>3%wt/wt)下,热变性是控制步骤,胶凝立即发生。这些结果表明,添加到牛奶中的盐的离子和缓冲特性将决定在经受高温、短时间处理(72°C 15 秒)的系统中乳清蛋白的天然状态与变性状态和胶凝。