Unilever Research and Development, Port Sunlight, Quarry Road East, Bebington, Wirral CH62 4ZD, UK.
ISIS, STFC, Rutherford Appleton Laboratory, Chilton, Didcot, Oxon OX1 0QX, UK.
J Colloid Interface Sci. 2016 Sep 15;478:81-7. doi: 10.1016/j.jcis.2016.06.002. Epub 2016 Jun 2.
The adsorption behaviour of mixtures of the proteins β-casein and hydrophobin at the hydrophilic solid-liquid surface have been studied by neutron reflectivity. The results of measurements from sequential adsorption and co-adsorption from solution are contrasted. The adsorption properties of protein mixtures are important for a wide range of applications. Because of competing factors the adsorption behaviour of protein mixtures at interfaces is often difficult to predict. This is particularly true for mixtures containing hydrophobin as hydrophobin possesses some unusual surface properties. At β-casein concentrations ⩾0.1wt% β-casein largely displaces a pre-adsorbed layer of hydrophobin at the interface, similar to that observed in hydrophobin-surfactant mixtures. In the composition and concentration range studied here for the co-adsorption of β-casein-hydrophobin mixtures the adsorption is dominated by the β-casein adsorption. The results provide an important insight into how the competitive adsorption in protein mixtures of hydrophobin and β-casein can impact upon the modification of solid surface properties and the potential for a wide range of colloid stabilisation applications.
通过中子反射率研究了亲水性固-液表面上β-酪蛋白和疏水蛋白混合物的吸附行为。对比了从溶液中顺序吸附和共吸附的测量结果。蛋白质混合物的吸附特性对于广泛的应用非常重要。由于竞争因素，蛋白质混合物在界面处的吸附行为通常难以预测。对于含有疏水蛋白的混合物尤其如此，因为疏水蛋白具有一些不寻常的表面特性。在β-酪蛋白浓度 ⩾0.1wt%的情况下，β-酪蛋白在界面上大量取代了预先吸附的疏水蛋白层，这与在疏水蛋白-表面活性剂混合物中观察到的情况类似。在研究的共吸附β-酪蛋白-疏水蛋白混合物的组成和浓度范围内，吸附主要由β-酪蛋白的吸附决定。研究结果深入了解了疏水蛋白和β-酪蛋白在蛋白质混合物中的竞争吸附如何影响固体表面性质的修饰以及胶体稳定化应用的广泛潜力。
