Temperature-orientation changes in ROS-oxidized egg white protein conformation modulate the thermal aggregation...

Area of Science:

• Food Science
• Protein Chemistry
• Biochemistry

Background:

• Egg white protein (EWP) aggregation is crucial for food processing.
• Understanding the impact of reactive oxygen species (ROS) on EWP thermal behavior is essential for optimizing egg product quality.
• Protein unfolding and subsequent interactions influence aggregation kinetics and structure.

Purpose of the Study:

• To investigate the effect of ROS on the thermal aggregation of EWP at varying temperatures.
• To elucidate the structural and hydrophobic changes during EWP heat-induced aggregation.
• To assess the anti-aggregation efficacy of oxidized EWP.

Main Methods:

• Turbidity measurements to monitor aggregation.
• Particle size analysis to characterize aggregate formation.
• Differential scanning calorimetry (DSC) for thermal stability assessment.
• Hydrophobicity assays.
• Raman spectroscopy for structural analysis.

Main Results:

• EWP turbidity and particle size changes correlated with protein unfolding and interactions.
• Aggregate structure evolved from fiber-like to network-like with increasing temperature.
• Oxidation significantly increased EWP thermal stability.
• Surface hydrophobicity increased dramatically upon aggregation (249.93 to 2748.10).
• Oxidized EWP exhibited significant anti-aggregation properties, particularly at 72°C, due to exposed hydrophobic groups.

Conclusions:

• ROS modify EWP aggregation behavior, enhancing thermal stability.
• Oxidation-induced structural changes, including hydrophobic group exposure, inhibit aggregation.
• Findings offer theoretical support for improving thermal processing of egg products.