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Net charge affects morphology and visual properties of ovalbumin aggregates

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Author: Weijers, M. · Broersen, K. · Barneveld, P.A. · Cohen Stuart, M.A. · Hamer, R.J. · Jongh, · Visschers, R.W.
Institution: TNO Kwaliteit van Leven
Source:Biomacromolecules, 11, 9, 3165-3172
Identifier: 241083
doi: doi:10.1021/bm800751e
Keywords: Nutrition · Food technology · Agglomeration · Chemical engineering · Chromatographic analysis · Electrophoresis · Morphology · Optical properties · Turbidity · Aggregate morphologies · Degree of branching · Net charges · Ovalbumin · Transmission electrons · Turbidity measurements · Visual appearances · Visual properties · Aggregates · ovalbumin · article · chemical modification · controlled study · disulfide bond · gel permeation chromatography · heating · incubation time · morphology · particle size · pH · physical chemistry · polyacrylamide gel electrophoresis · priority journal · protein aggregation · protein structure · rigidity · transmission electron microscopy · turbidity · Animals · Electrophoresis, Polyacrylamide Gel · Microscopy, Electron · Nephelometry and Turbidimetry · Ovalbumin · Pliability · Precipitation · Protein Conformation · Solubility · Static Electricity


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.