Quantitative proteomics provides a new perspective on the mechanism of network structure depolymerization during egg...

Area of Science:

• Food science
• Protein chemistry
• Colloid science

Background:

• Egg white (EW) is a common colloidal system prone to thinning during storage.
• Understanding the molecular mechanisms behind EW thinning is crucial for food stability.

Purpose of the Study:

• To investigate the mechanisms of EW thinning and protein depolymerization.
• To analyze changes in protein composition and molecular structure during EW storage.

Main Methods:

• Rheological analysis to measure viscoelasticity.
• Gel system analysis to observe protein arrangement.
• Molecular characteristic analysis (particle size, sulfhydryl content, disulfide bonds).
• Quantitative proteomic analysis to identify protein abundance changes.

Main Results:

• EW viscoelasticity significantly declined during storage.
• Protein depolymerization involved dissociation of skeleton proteins and decreased particle size.
• Increased disulfide bonds enhanced electrostatic forces, hindering aggregation and reducing hydrophobicity.
• Reduced abundance of β-ovomucin (OVO) was identified as a potential direct cause of thinning.
• Specific proteins were found to aggregate during later storage stages.

Conclusions:

• EW thinning is linked to protein depolymerization and structural changes.
• β-ovomucin plays a key role in maintaining EW structure and stability.
• Storage-induced alterations in protein aggregation and molecular interactions affect EW properties.