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Structure of beta-casein layers at the air/solution interface: atomic force microscopy studies of transferred layers.

We report the nanoscale structural changes associated with the interfacial gelation of adsorbed beta-casein layers as a function of aging time. Adsorbed layers were transferred to solid supports and imaged by atomic force microscopy. The aging of the layer was accompanied by the formation of distinct disk-shaped protein nanoparticles ( approximately 20 nm in diameter). Under conditions where a gelled layer was expected (from previous interfacial rheology experiments), we observed ordering of the particles and the formation of elongated aggregates or linear rows. Brewster angle microscopy images were also obtained during the adsorption and gelation processes and during the degradation of the protein layer following addition of the surfactant sodium dodecyl sulfate (SDS). If SDS was added prior to interfacial protein gelation, the layer developed a foamlike morphology consistent with a fluid interfacial protein layer. However, if SDS was added after gelation, the protein layer was observed to fracture, consistent with the behavior of a solid phase.