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Films et bulles de protéines solubles : structure, interactions et perméabilité au gaz

Abstract : Thin films of soluble proteins are good model systems to study the interactions between two bubbles, and to discuss the stability of protein foams. During this work, we have shown that the stability, structure and permeability to air of the films are determined by the properties of the protein layers adsorbed at the air/water interface. We managed to control the formation of a protein black film by adjusting the parameters of the bulk (pH, ionic strength etc.) and we determined its molecular organization by X-ray reflectivity. We have also shown that protein bubbles are gradually surrounded by an insoluble shell as they shrink under the effect of Ostwald ripening. The kinetics of this phenomenon is especially slow and has been explained as a function of the dynamic structure and the rheology of the protein network that forms the wall of the bubbles. In addition, we proposed a new experimental device for measuring the interactions that take part within protein films. Finally, we tried to see whether there is a correlation between the properties of individual protein films and bubbles, and the behaviour of macroscopic foams obtained in analogous conditions. Experimentally, we found that this correlation was not as obvious as expected because the structure of the adsorbed protein layers depends closely on the mechanical events they had been exposed to. In the last part, we have determined the architecture of a new type of complex films stabilized by amphiphilic cyclodextrins. We have used the confined geometry of black films for studying the hydration properties of these objects.
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Submitted on : Wednesday, April 6, 2005 - 4:38:44 PM
Last modification on : Friday, March 5, 2021 - 2:59:18 PM
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  • HAL Id : tel-00008960, version 1

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Caroline Sultanem. Films et bulles de protéines solubles : structure, interactions et perméabilité au gaz. Matière Condensée [cond-mat]. Université Paris Sud - Paris XI, 2004. Français. ⟨tel-00008960⟩

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