Adsorption Kinetics and Elutability of α-Lactalbumin, β-Casein, β-Lactoglobulin, and Bovine Serum Albumin at Hydrophobic and Hydrophilic Interfaces

Ellipsometric Study of Bovine Serum Albumin Adsorbed onto Ti/TiO2 Electrodes

“…Similarly to what is proposed here, Krisdhasima et al (44) found experimentally two different kinetics processes for ␣-lactalbumin, ␤-casein, ␤-lactoglobulin, and BSA adsorbed on silica surfaces of low and high hydrophobicity. They could fit the data with a theoretical model by assuming that in a first step the protein molecules attach to the surface without changing their conformation, and in a second step, they undergo conformational changes.…”

The Adsorption–Desorption Cycle. Reversibility of the BSA–Silica System

“…For example, the system of bovine serum albumin (BSA)-silica particles has been extensively investigated. The studies mainly concern the dependence of the adsorbed amount on the pH (10), the ionic strength (10) or presence of displacing agents (11), the kinetics of adsorption and desorption (12,13), or the structure of adsorbed protein molecules (14)(15)(16). Some general trends have emerged: BSA adsorbs on silica particles even under nonfavorable electrostatic interactions; it can be desorbed by changing the pH away from the isoelectric point of the protein and by increasing the ionic strength; the driving force of the adsorption process is related to the structural changes in the adsorbing BSA molecules.…”

Building a working understanding of protein adsorption with model systems and serendipity

“…There we set up a system for in situ detection of protein adsorption by ellipsometry [1] and began quantifying surface and protein properties affecting the rate and extent of protein adsorption from single-protein solutions [2][3][4][5][6][7]. We worked mainly with the milk proteins ˛-lactalbumin, ˇ-lactoglobulin, BSA, and ˇ-casein.…”