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High pressure thermal denaturation kinetics of whey proteins.

机译:乳清蛋白的高压热变性动力学。

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摘要

Effect of high pressure processing of milk on denaturation of whey proteins was investigated. Pressure and temp. dependent denaturation kinetics were determined separately. In a detailed kinetic study, whey protein isolate was treated under isobaric (200-800 MPa) and isothermal conditions (-2 to 70degC), and the resulting degree of denaturation of beta-lactoglobulin A and B and alpha-lactalbumin was analysed. Kinetic parameters of denaturation were estimated using a 1 step non-linear regression method which allowed a global fit of the whole data set. The isobaric isothermal denaturation of beta-lactoglobulin and alpha-lactalbumin was found to follow 3rd and 2nd order kinetics, respectively. Isothermal pressure denaturation of both beta-lactoglobulin fractions did not differ significantly and were characterized by a decrease in activation vol. with increasing temp. from -10 to approx. -30 ml/mol, which demonstrates that the denaturation rate is accelerated with increasing temp. The activation energy of approx. 70-100 kJ/mol obtained for beta-lactoglobulin A and B was not dependent to a great extent on the pressure; this indicates that at pressures >200 MPa, the denaturation rate is limited by the aggregation rate, while pressure forces the molecules to unfold.
机译:研究了牛奶的高压处理对乳清蛋白变性的影响。压力和温度依赖的变性动力学分别确定。在详细的动力学研究中,乳清蛋白分离物在等压(200-800 MPa)和等温条件(-2至70摄氏度)下处理,并分析了β-乳球蛋白A和B以及α-乳清蛋白的变性程度。使用第一步非线性回归方法估算变性的动力学参数,该方法可以对整个数据集进行全局拟合。发现β-乳球蛋白和α-乳清蛋白的等压等温变性分别遵循三级和二级动力学。两个β-乳球蛋白馏分的等温变性均无显着差异,其特征在于活化体积降低。随着温度的升高从-10到大约-30 ml / mol,这表明变性速率随着温度的升高而加快。活化能约为β-乳球蛋白A和B所获得的70-100 kJ / mol在很大程度上不依赖于压力。这表明在大于200 MPa的压力下,变性速率受聚集速率的限制,而压力迫使分子展开。

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