科研之友
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摘要
Ovalbumin is the main constituent of egg white protein. Improvements in the functional properties of ovalbumin are of great importance in the food industry. Therefore, in this article, the structural and functional properties of ovalbumin, which were glycated by dry-heating, were investigated. The micrographs showed that glycated ovalbumin was smaller and more homogeneous than native and dry-heated ovalbumin. Although changes in the random coil structure of ovalbumin measured by circular dichroism were mild, increased surface hydrophobicity and decreased tryptophan fluorescence intensity were observed following glycation. Glycation improved the stability against heat induced insolubility, emulsifying properties, water and oil binding capacity of ovalbumin. These results suggested that dry-heating glycation is a useful method for improving the functional properties of ovalbumin. The attention on the structural and functional changes in this work will be contributed to the understanding of the structure-function relationship. These insights would have important implications for the creation of desirable structure and functional properties of food products.
