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Slow dynamics and structure in jammed milk protein suspensions

机译:堵塞牛奶蛋白悬浮液中的动力学和结构

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The dynamic mechanical properties and the structure of dense suspensions of sodium caseinate were investigated using oscillatory shear rheology and confocal laser scanning microscopy, respectively. Caseins are the most abundant milk proteins and form in the absence of calcium phosphate small star-like particles with radii of about 10 nm. The viscosity increases strongly with increasing protein concentration above ~80 g L~(-1) due to jamming of the particles. The viscosity increase is stronger at lower temperatures, caused by a strong decrease in the terminal relaxation time with increasing temperature. Addition of calcium ions introduces an attractive interaction that induces phase separation above a critical calcium concentration. Increasing the CaCl_2 concentration leads to an increase in the terminal relaxation time, but to a decrease in the high frequency elastic modulus. The effect of adding CaCl_2 is stronger at higher temperatures.
机译:使用振荡剪切流变学和共聚焦激光扫描显微镜研究了动态力学性能和浓度酪蛋白钠的致密悬浮液。酪蛋白是最丰富的牛奶蛋白,并且在没有磷酸钙的小星形颗粒的情况下形成含有约10nm的半径。由于颗粒的干扰,粘度随着蛋白质浓度的增加而强烈增加〜80g L〜(-1)。粘度升高在较低温度下较强,由于终端松弛时间随着温度的升高而导致的终端松弛时间强。加入钙离子引入有吸引力的相互作用,其诱导高于临界钙浓度的相分离。增加CaCl_2浓度导致端子松弛时间的增加,但是高频弹性模量的降低。添加CaCl_2的效果在较高温度下更强。

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