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
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
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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