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Article Dans Une Revue Journal of Colloid and Interface Science Année : 2010

Self-similar assemblies of globular whey proteins at the air-water interface: Effect of the structure

Résumé

We investigated the structure of heat-induced assemblies of whey globular proteins using small angle neutron scattering (SANS), static and dynamic light scattering (SLS and DLS), and cryogenic transmission electron microscopy (Cryo-TEM). Whey protein molecules self-assemble in fractal aggregates with a structure density depending on the electrostatic interactions. We determined the static and dynamic properties of interfacial layer formed by the protein assemblies, upon adsorption and spreading at the air-water interface using surface film balance and interfacial dilatational rheology. Upon spreading, all whey protein systems show a power-law scaling behavior of the surface pressure versus concentration in the semi-dilute surface concentration regime, with an exponent ranging from 5.5 to 9 depending on the electrostatic interactions and the aggregation state. The dilatational modulus derived from surface pressure isotherms shows a main peak at 6-8 mN/m, generally considered to be the onset of a conformational change in the monolayer, and a second peak or a shoulder at 15 mN/m. Long-time adsorption kinetics give similar results for both the native whey proteins and the corresponding self-similar assemblies, with a systematic effect of the ionic strength

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Dates et versions

hal-02667000 , version 1 (31-05-2020)

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Najet Mahmoudi, Cedric Gaillard, François Boué, Monique Axelos M.A.V., Alain Riaublanc. Self-similar assemblies of globular whey proteins at the air-water interface: Effect of the structure. Journal of Colloid and Interface Science, 2010, 345 (1), pp.54-63. ⟨10.1016/j.jcis.2010.01.036⟩. ⟨hal-02667000⟩
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