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- W2022903721 abstract "Of the different biopolymers, most studies of adsorption have been made with proteins. As a result of their marked polar/non-polar composition, proteins adsorb strongly at most of the interfaces commonly studied. This property is not shared by polysaccharides and polynucleotides to the same extent. The adsorption of these biopolymers has therefore been comparatively little studied, and requires very specific types of interface. The use of proteins and fluid interfaces provides certain advantages for arriving at a general understanding of the mechanism of the adsorption process. Firstly, at fluid interfaces, it is possible to measure parameters such as area per molecule precisely and to verify that the interface is clean and free from surface-active impurities. Secondly, proteins are useful because, when they are pure, they are of constant size, unlike most polymer preparations. In addition, their relatively low diffusion coefficients facilitate the measurements required to elucidate the role of diffusion in adsorption. These measurements are very sensitive to the presence of impurities, both in the protein sample and in the two phases that form the interface. Great care is required to ensure purity as well as reproducible diffusion conditions. Other aspects of the adsorption process can be studied using the film balance to calculate the adsorption kinetics from measurements of the rate of increase of area at constant interfacial pressure. In this way, information may be gained about the nature of the transition complex in adsorption. The same techniques can be used to gain corresponding information about the desorption process. At moderate interfacial pressures, the activation energy barrier to adsorption is relatively low compared with that for desorption." @default.
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- W2022903721 title "Adsorption of biopolymers" @default.
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