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Proteomic analysis of egg white proteins during storage
Dileep A Omana1, Yue Liang, Nat N V Kav
1Department of Agricultural, Food and Nutritional Science, University of Alberta, Edmonton, Alberta, Canada.
Proteomics
|December 25, 2010
Summary
Egg white thinning during storage is linked to changes in protein levels. Ovalbumin and clusterin degradation, influenced by proteolysis and pH, contribute to this common phenomenon.
Area of Science:
- Food Science
- Biochemistry
- Proteomics
Background:
- Egg white thinning is a common post-storage phenomenon affecting egg quality.
- Understanding the molecular mechanisms behind egg white thinning is crucial for the food industry.
Purpose of the Study:
- To investigate the proteome-level changes in egg white proteins during storage.
- To identify key proteins involved in the egg white thinning process.
Main Methods:
- White-shell eggs were stored at ambient temperature (22 ± 2 °C).
- Proteomic analysis was performed to quantify changes in egg white protein abundance over time.
- Visual observation of egg white thinning was correlated with proteomic data.
Main Results:
- Egg white thinning was visually observed after 20 days of storage.
- Significant changes in the abundance of ovalbumin, clusterin, ovoinhibitor, ovotransferrin, and prostaglandin D2 synthase were detected.
- Clusterin abundance showed continuous change throughout the storage period.
Conclusions:
- Increased concentrations of clusterin and ovoinhibitor, alongside changes in ovalbumin, likely contribute to egg white thinning.
- Degradation of ovalbumin and clusterin, potentially due to proteolysis and increased pH, is a key factor in egg white thinning.
