# Structural modification of egg white proteins enhances electrostatic complexation with sodium alginate and hydrogel particle formation: mechanistic insights and functional applications

## TL;DR

Researchers modified egg white proteins to make them more flexible, enabling better binding with sodium alginate to form stable hydrogel particles that can protect fish oil from oxidation.

## Contribution

The study introduces a method to enhance the structural flexibility of egg white proteins for improved hydrogel formation and bioactive compound stabilization.

## Key findings

- pH 13 and 50 °C treatment maximized EWP structural flexibility and electrostatic complexation with sodium alginate.
- Modified EWP formed uniform hydrogel particles that effectively encapsulated fish oil emulsions.
- Encapsulated fish oil showed improved oxidative and dispersion stability compared to unencapsulated emulsions.

## Abstract

Many bioactive compounds, such as fish oil, are prone to oxidation, which limits their incorporation into functional foods. Egg white proteins (EWP) have notable antioxidant properties, making them promising candidates for stabilizing such compounds, but their compact globular structure limits flexibility and reduces their ability to form stable hydrogel particles with polysaccharides. Based on this, the purpose of this study was to explore the structural modification of EWP via pH-shifting and heat treatment to enhance their electrostatic complexation with sodium alginate (NaAlg) and subsequent hydrogel particle formation. We compared different modification treatments and found that treatment at pH 13 and 50 °C produced the optimal effect, effectively exposing tryptophan and tyrosine residues and increasing the structural flexibility of EWP while maintaining its ionization properties. These conformational changes promoted strong electrostatic interactions with NaAlg, resulting in uniformly distributed hydrogel particles. Confocal microscopy confirmed the encapsulation of fish oil emulsion within the hydrogel particles, and the formed particles exhibited improved oxidative stability and dispersion compared to simple dispersions. These enhancements were attributed to both the physical encapsulation within the hydrogel matrix and the intrinsic antioxidant properties of EWP. This work demonstrates how increasing protein flexibility can facilitate polysaccharide complexation and hydrogel formation, providing mechanistic insights and guiding potential applications for compact globular proteins in functional food systems.

Image 1

•Egg white proteins (EWP) were modified via pH-shifting and heat treatment.•Hydrophobicity and structural flexibility of EWP increased after modification.•Modified EWP and NaAlg formed uniform, stable hydrogel particles.•Fish oil emulsions could be encapsulated within the MEWP-rich particles.•Filled hydrogel particles improved the oxidative and dispersion stability of the encapsulated fish oil emulsion compared to a simple emulsion.

Egg white proteins (EWP) were modified via pH-shifting and heat treatment.

Hydrophobicity and structural flexibility of EWP increased after modification.

Modified EWP and NaAlg formed uniform, stable hydrogel particles.

Fish oil emulsions could be encapsulated within the MEWP-rich particles.

Filled hydrogel particles improved the oxidative and dispersion stability of the encapsulated fish oil emulsion compared to a simple emulsion.