In the present paper, an improved multiscale modeling aimed at describing membrane fouling in the UltraFiltration (UF) process was proposed. Some of the authors of this work previously published a multiscale approach to simulate ultrafiltration of Bovine Serum Albumin (BSA) aqueous solutions. However, the noncovalent interactions between proteins and the membrane surface were not taken into account in the previous formulation. Herein, the proteins-surface interactions were accurately computed by first-principle-based calculations considering also the effect of pH. Both the effective surface of polysulfone (PSU) and the first layer of proteins adsorbed on the membrane surface were accurately modeled. Different from the previous work, the equilibrium distance between proteins was calculated and imposed as lower bound to the protein-protein distances in the compact deposit accumulated on the membrane surface. The computed BSA surface charges were used to estimate the protein potential and the charge density, both necessary to formulate a forces balance at microscopic scale. The protein surface potential was compared with Z-potential measurements of BSA aqueous solution, and a remarkable agreement was found. Finally, the overall additional resistance, as due to both the compact and loose layers of the deposit, was computed, thus allowing the final transition to a macroscopic scale, where an unsteady-state mass transfer model was formulated to describe the behavior of a typical dead-end UF process. A good agreement between simulated and experimental permeate flux decays was observed.

Interactions between Proteins and the Membrane Surface in Multiscale Modeling of Organic Fouling

Curcio Stefano
2018-01-01

Abstract

In the present paper, an improved multiscale modeling aimed at describing membrane fouling in the UltraFiltration (UF) process was proposed. Some of the authors of this work previously published a multiscale approach to simulate ultrafiltration of Bovine Serum Albumin (BSA) aqueous solutions. However, the noncovalent interactions between proteins and the membrane surface were not taken into account in the previous formulation. Herein, the proteins-surface interactions were accurately computed by first-principle-based calculations considering also the effect of pH. Both the effective surface of polysulfone (PSU) and the first layer of proteins adsorbed on the membrane surface were accurately modeled. Different from the previous work, the equilibrium distance between proteins was calculated and imposed as lower bound to the protein-protein distances in the compact deposit accumulated on the membrane surface. The computed BSA surface charges were used to estimate the protein potential and the charge density, both necessary to formulate a forces balance at microscopic scale. The protein surface potential was compared with Z-potential measurements of BSA aqueous solution, and a remarkable agreement was found. Finally, the overall additional resistance, as due to both the compact and loose layers of the deposit, was computed, thus allowing the final transition to a macroscopic scale, where an unsteady-state mass transfer model was formulated to describe the behavior of a typical dead-end UF process. A good agreement between simulated and experimental permeate flux decays was observed.
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/20.500.11770/286613
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