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Ultrathin Micellar Foam Films of Sodium Caseinate Protein Solutions
Lena Hassan1, Chenxian Xu1, Michael Boehm2
1Department of Chemical Engineering, University of Illinois Chicago, 929 West Taylor Street, Chicago, Illinois 60607, United States.
Abstract:
Sodium caseinates (NaCas), derived from milk proteins called caseins, are often added to food formulations as emulsifiers, foaming agents, and ingredients for producing dairy products. In this contribution, we contrast the drainage behavior of single foam films made with micellar NaCas solutions with well-established features of stratification observed for the micellar sodium dodecyl sulfate (SDS) foam films. In reflected light microscopy, the stratified SDS foam films display regions with distinct gray colors due to differences in interference intensity from coexisting thick-thin regions. Using IDIOM (interferometry digital imaging optical microscopy) protocols we pioneered for mapping nanotopography of foam films, we showed that drainage via stratification in SDS films proceeds by the expansion of flat domains that are thinner than surrounding by a concentration-dependent step-size, and nonflat features (nanoridges and mesas) form at the moving front. Furthermore, stratifying SDS foam films show stepwise thinning, such that the step-size and terminal film thickness decrease with concentration. Here we visualize the nanotopography in protein films with high spatiotemporal resolution using IDIOM protocols to address two long-standing questions. Do protein foam films formulated with NaCas undergo drainage via stratification? Are thickness transitions and variations in protein foam films determined by intermicellar interactions and supramolecular oscillatory disjoining pressure? In contrast with foam films containing micellar SDS, we find that micellar NaCas foam films display just one step, nonflat and noncircular domains that expand without forming nanoridges and a terminal thickness that increases with NaCas concentration. We infer that the differences in adsorbing and self-assembling unimers triumph over any similarities in the structure and interactions of their micelles.
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