Abstract
The aim of the present study was to investigate the chemical and structural changes in preserved white egg during pickled by vacuum technology. In order to evaluate the changes of preserved egg white during its salted period, sulfhydryl group, disulfide bond contents, and surface hydrophobicity were measured. Fourier transformation infrared spectroscopy and circular dichroism analysis were performed by considering changes of the secondary structural elements, the protein components of egg white was also studied in more detail by electrophoresis. Results showed that the sulfhydryl group and surface hydrophobicity were increased with increasing salting time, whereas a decrease in the disulfide bond contents was observed. Regarding the secondary structure analysis, a decrease in α-helices and β-turns were accompanied by increases in β-sheets and random coils, which indicating a decrease in non-random structure while ever increasing of unordered structure. Electrophoresis shows no significant differences in protein patterns among fresh egg white and samples salting for up to 4 days. Disappearance of most protein was at the 5th day. Single band of ovalbumin can be readily observed from the 6th day to the ripening period finished. Our findings reveal that high pH could induce duck egg white protein aggregation when salting eggs in strong alkaline solution for a long time.
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