Abstract
A Multiangle laser photometer and a dynamic light scattering spectrophotometer were used to characterize the aggregation behavior and gel network structure of elastic and less elastic gels of ovalbumin. Ovalbumin formed opaque and less elastic gels in 50 mM phosphate buffer (pH 7.0). However, succinylated ovalbumin formed transparent and elastic gels. Heat-induced ovalbumin protein formed high molecular weight and polydisperse aggregates. Succinylation of the protein contributed to formation of lower molecular weight polymers with a narrow molecular size distribution during subsequent heat gelation. The root mean square and hydrodynamic radii of the protein polymers indicated that the elastic gel consisted of a more extended protein polymer network compared to that of the less elastic gel. The aggregation behavior of denatured ovalbumin appeared to play a crucial role in the subsequent gelling process of the proteins.
Published Version
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