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首页> 外文期刊>Journal of Agricultural and Food Chemistry >COADSORPTION OF BETA-CASEIN AND BOVINE SERUM ALBUMIN AT THE AIR-WATER INTERFACE FROM A BINARY MIXTURE
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COADSORPTION OF BETA-CASEIN AND BOVINE SERUM ALBUMIN AT THE AIR-WATER INTERFACE FROM A BINARY MIXTURE

机译：β-酪蛋白和牛血清白蛋白在二元混合物在空气界面的共吸附

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摘要

Competitive adsorption of bovine serum albumin (BSA) and beta-casein from binary solutions to the air-water interface have been studied. Adsorption of these proteins followed a kinetically controlled, instead of a Langmuirian-type thermodynamically controlled, competitive adsorption mechanism. Molecular area calculations indicated that the excluded area between protein molecules in the binary protein film at the air-water interface was greater than that in saturated monolayers of single protein systems, indicating thermodynamic incompatibility of mixing of these proteins. Adsorption of 3 molecules of BSA excluded adsorption of 16 molecules of beta-casein from the interface and vice versa. Sequential adsorption experiments showed that beta-casein can displace beta-casein from the interface, whereas it cannot displace adsorbed BSA. In contrast, BSA can neither displace beta-casein nor exchange with adsorbed BSA. The results showed that the protein component that arrives first to the interface adsorbs first, and the late-arriving protein component cannot displace the adsorbed component regardless of its surface active properties.
机译：研究了牛血清白蛋白（BSA）和β-酪蛋白从二元溶液到空气-水界面的竞争性吸附。这些蛋白质的吸附遵循动力学控制的方式，而不是Langmuirian型热力学控制的竞争性吸附机制。分子面积计算表明，在空气-水界面的二元蛋白膜中的蛋白分子之间的排除面积大于单个蛋白系统的饱和单层中的排除面积，表明这些蛋白混合的热力学不相容性。 3个BSA分子的吸附排除了16个β-酪蛋白分子从界面的吸附，反之亦然。顺序吸附实验表明，β-酪蛋白可以从界面上置换β-酪蛋白，而不能置换吸附的BSA。相反，BSA既不能取代β-酪蛋白，也不能与吸附的BSA交换。结果表明，最先到达界面的蛋白质成分首先被吸附，而迟到的蛋白质成分无论其表面活性如何都无法取代被吸附的成分。

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