Foam structure

ISFP-R26

Protein adsorption at the air–water: when the charge sign matters

When proteins adsorb to the air–water interface, the magnitude of their charge affects the formation and properties of the adsorption layer. What about the sign of the charge ?

Proteins adsorb from aqueous solutions to the air–water interface, and lower the interfacial tension. Due to their acidic and/or basic groups, their net charge varies with pH, depending on their isoelectric point. Coulombic effects make the adsorption process and the properties of the adsorption layer sensitive to the net charge. Upon evaporation of the protein solution, the water flow across the interface results in advection, i.e. protein transport towards the interface, which may also affect adsorption.

Neutron reflectometry and ellipsometry show that when lysozyme or ovalbumin adsorbs at the air–water interface, it is necessary to combine a positive protein net charge and the presence of advection to obtain multilayers. When these conditions are not both fulfilled, stationary monolayers are observed. We tried to simulate the experimental results using a model involving advection, which tends to accumulate protein at the interface, and diffusion, which opposes to accumulation and tend to flatten the concentration gradient. This model cannot reproduce at the same time the shape and dimensions of spatial and temporal concentration gradients.

Adsorption mechanism

Both a positive charge and an evaporation flux are required for the formation of multilayers at air-water interfaces

This work suggests that intermolecular interactions depending on the sign of the protein net charge should be considered to explain the properties of adsorption layers.

Collaborations

Read more

Pasquier, C., Pezennec, S., Bouchoux, A., Cabane, B., Lechevalier, V., Le Floch-Fouéré, C., Paboeuf, G., Pasco, M., Dollet, B., Lee, L.-T. & Beaufils, S. (2021) Protein Transport upon Advection at the Air/Water Interface: When Charge Matters. Langmuir 37, 12278–12289. https://dx.doi.org/10.1021/acs.langmuir.1c01591. https://hal.inrae.fr/hal-03375385

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Date de modification : 30 janvier 2023 | Date de création : 12 décembre 2022 | Rédaction : MH Famelart