![Sample our Environment & Agriculture journals, sign in here to start your access, latest two full volumes FREE to you for 14 days]({"type":"image" , "src" : "/sda/5934/TOC-Subject-Sample-2021-Environment-Agriculture.jpg"})
The model systems used in this study were selected so as to obtain a variety of hydrophobicities and electrokinetic charge densities of proteins and sorbent surfaces, and a range of protein structural stabilities. Adsorption from solutions of a single protein as well as from protein mixtures was studied, both in the initial and final stage of the process. Information has been inferred from streaming potential measurements, reflectometry and solution depletion measurements. The tendency of a surface to adsorb proteins increases with increasing hydrophobicity and increasing charge contrast between the protein and the surface. Furthermore, a structurally weaker protein has a higher adsorption affinity. In line with this, adsorption competition between various proteins at a given surface is strongly influenced by electrostatic interaction and by their conformational stability.
Notes
Corresponding author.
On leave of absence from the Department of Industrial Chemistry, Nihon University, Izumi‐Cho 1–2–1, Narashino‐shi, Chiba 275. Japan.
On leave of absence from the Department of Applied Chemistry, Hiroshima University, Higashi‐Hiroshima, Japan.