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Adsorption of Milk Proteins (beta Casein and beta-Lactoglobulin) and BSA onto Hydrophobic Surfaces

Year: 2017

Journal: Materials, Volume 10, AUG

Authors: Perez-Fuentes, Leonor; Drummond, Carlos; Faraudo, Jordi; Bastos-Gonzalez, Delfi

Keywords: proteins; QCM; MD simulations; hydrophobic effect; ion condensation; electrokinetic mobility

Here, we study films of proteins over planar surfaces and protein-coated microspheres obtained from the adsorption of three different proteins (beta-casein, beta-lactoglobulin and bovine serum albumin (BSA)). The investigation of protein films in planar surfaces is performed by combining quartz crystal microbalance (QCM) and atomic force microscopy (AFM) measurements with all-atomic molecular dynamics (MD) simulations. We found that BSA and beta-lactoglobulin form compact monolayers, almost without interstices between the proteins. However, beta-casein adsorbs forming multilayers. The study of the electrokinetic mobility of protein-coated latex microspheres shows substantial condensation of ions from the buffer over the complexes, as predicted from ion condensation theories. The electrokinetic behavior of the latex-protein complexes is dominated by the charge of the proteins and the phenomenon of ion condensation, whereas the charge of the latex colloids plays only a minor role.