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Kinetics of denaturation and aggregation of whey proteins in skim milk heated in an ultra-high temperature (UHT) pilot plant

机译:超高温(UHT)中试工厂加热的脱脂牛奶中乳清蛋白变性和聚集的动力学

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Skim milk was subjected to various temperature-time (70-130deg C for 3-1800 s) treatments in a pilot-scale ultra-high temperature (UHT) plant using a direct steam injection (DSI) system. The rates of denaturation and aggregation of beta-lactoglobulin (beta-lg) and alpha-lactalbumin (alpha-la) were determined by quantitative PAGE while that of immunoglobulin G (IgG) was determined by affinity chromatography. The order of reaction, the rate constant and the activation energy were determined for the denaturation of beta-lg, alpha-la and IgG using non-linear regression methods. The kinetic parameters obtained for beta-lg and alpha-la showed a marked temperature dependence. Aggregation of beta-lg mainly involved the formation of intermolecular disulphidelinkages at all temperatures studied, while the aggregation of alpha-la, particularly below 80deg C, appeared to also involve hydrophobic interactions. The kinetic parameters obtained for beta-lg aggregation, due to disulphide bond formation, were similar to those observed for beta-lg denaturation.
机译:使用直接蒸汽注入(DSI)系统在中试规模的超高温(UHT)工厂中对脱脂牛奶进行各种温度-时间处理(70-130摄氏度,持续3-1800 s)。 β-乳球蛋白(β-1g)和α-乳白蛋白(α-1a)的变性和聚集速率通过定量PAGE确定,而免疫球蛋白G(IgG)的亲和色谱确定。使用非线性回归方法确定β-Ig,α-1a和IgG的变性的反应顺序,速率常数和活化能。对于β-1g和α-1a获得的动力学参数显示出明显的温度依赖性。 β-Ig的聚集主要涉及在所有研究温度下分子间二硫键的形成,而α-1a的聚集,特别是在80℃以下,似乎也涉及疏水相互作用。由于形成二硫键,β-Ig聚集获得的动力学参数与β-Ig变性观察到的动力学参数相似。

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