Print Email Facebook Twitter Net charge affects morphology and visual properties of ovalbumin aggregates Title Net charge affects morphology and visual properties of ovalbumin aggregates Author Weijers, M. Broersen, K. Barneveld, P.A. Cohen Stuart, M.A. Hamer, R.J. de Jongh, H.H.J. Visschers, R.W. TNO Kwaliteit van Leven Publication year 2008 Abstract The effect of ovalbumin net charge on aggregate morphology and visual properties was investigated using chromatography, electrophoresis, electron microscopy, and turbidity measurements. A range of differently charged ovalbumin variants (net charge ranging from -1 to -26 at pH 7) was produced using chemical engineering. With increasing net charge, the degree of branching and flexibility of the aggregates decreased. The turbidity of the solutions reflected the aggregate morphology that was observed with transmission electron microscopy. Increasing the stiffness of the aggregates transformed the solutions from turbid to transparent. Artificially shielding the introduced net charge by introducing salt in the solution resulted in an aggregate morphology that was similar to that for low-net-charge variants. The morphology of heat-induced aggregates and the visual appearance of the solutions were significantly affected by net charge. We also found that the morphology of ovalbumin aggregates can be rapidly probed by high-throughput turbidity experiments. © 2008 American Chemical Society. Subject NutritionFood technologyAgglomerationChemical engineeringChromatographic analysisElectrophoresisMorphologyOptical propertiesTurbidityAggregate morphologiesDegree of branchingNet chargesOvalbuminTransmission electronsTurbidity measurementsVisual appearancesVisual propertiesAggregatesovalbuminarticlechemical modificationcontrolled studydisulfide bondgel permeation chromatographyheatingincubation timemorphologyparticle sizepHphysical chemistrypolyacrylamide gel electrophoresispriority journalprotein aggregationprotein structurerigiditytransmission electron microscopyturbidityAnimalsElectrophoresis, Polyacrylamide GelMicroscopy, ElectronNephelometry and TurbidimetryOvalbuminPliabilityPrecipitationProtein ConformationSolubilityStatic Electricity To reference this document use: http://resolver.tudelft.nl/uuid:6f18508f-d5d3-4f12-ad19-8b01d5013ecc DOI https://doi.org/10.1021/bm800751e TNO identifier 241083 ISSN 1525-7797 Source Biomacromolecules, 9 (11), 3165-3172 Document type article Files To receive the publication files, please send an e-mail request to TNO Library.