Print Email Facebook Twitter Assessing the extent of protein intermolecular interactions at air-water interfaces using spectroscopic techniques Title Assessing the extent of protein intermolecular interactions at air-water interfaces using spectroscopic techniques Author de Jongh, H.H.J. Wierenga, P.A. TNO Kwaliteit van Leven Publication year 2006 Abstract There is an ongoing debate about whether a protein surface film at an air-water interface can be regarded as a gelled layer. There is literature reporting that such films show macroscopic fracture behavior and a rheology comparable to three-dimensional protein bulk-networks. If this is the case, a complete description of the formation of adsorbed layers should include a transition from single, freely moving proteins to a gelled layer. This report presents studies using spectroscopic techniques, such as infrared, fluorescence and neutron spectroscopy, or ellipsometry, to derive molecular insight in situ to substantiate the intermolecular networking in surface films of chicken egg ovalbumin. It is concluded that protein films, generated by equilibrium adsorption from the bulk, behave as a densely packed colloidal repulsive particle system, where the proteins still have a significant rotational mobility, have a predominantly retained globular fold, and show distinct (lateral) diffusion. Applied stresses on the surface film (by compressions of the interface) may result in protein denaturation and aggregation. This process renders a surface film from a colloidal particle into that of a gelled system. © 2006 Wiley Periodicals, Inc. Subject NutritionFood technologyAir-water interfaceEllipsometryFluorescenceInfraredNeutron reflectionProteinAgglomerationBiofilmsColloidsEllipsometryRheologySpectroscopic analysisSurface chemistryAir-water interfacesDistinct (lateral) diffusionRetained globular foldProteinsovalbuminwateradsorptionairarticlechickencompressioneggellipsometryequilibrium constantfluorescence spectroscopyinfrared spectroscopyneutron radiationprotein aggregationprotein analysisprotein interactionAirColloidsGelsOvalbuminProtein ConformationProteinsProteomicsSpectrometry, FluorescenceSpectrophotometry, InfraredSurface PropertiesSurface TensionTime FactorsWater To reference this document use: http://resolver.tudelft.nl/uuid:fcd2de97-c04e-4c04-b727-fef0b454c8d6 DOI https://doi.org/10.1002/bip.20519 TNO identifier 239352 ISSN 0006-3525 Source Biopolymers, 82 (4), 384-389 Document type article Files To receive the publication files, please send an e-mail request to TNO Library.