Whey Protein Peptides Have Dual Functions: Bioactivity and Emulsifiers in Oil-In-Water Nanoemulsion

Area of Science:

• Food Science
• Protein Chemistry
• Colloid Science

Background:

• Whey protein isolate (WPI) is a rich source of bioactive peptides.
• Nanoemulsions are widely used in food and pharmaceutical industries.
• The emulsifying properties of WPI-derived peptides are not fully understood.

Purpose of the Study:

• To investigate the use of WPI-derived bioactive peptide fractions as emulsifiers in nanoemulsions.
• To determine the effect of peptide size, enzyme type, concentration, and storage temperature on nanoemulsion formation and stability.

Main Methods:

• Fractionation of WPI bioactive peptides by ultrafiltration.
• Preparation of nanoemulsions using different peptide fractions as emulsifiers.
• Characterization of nanoemulsion properties (droplet size, stability) under various conditions.

Main Results:

• Peptide size significantly impacts emulsifying performance; smaller fractions (<10 kDa) showed poor surface activity.
• Larger peptide fractions (>10 kDa) formed stable nanoemulsions (174–196 nm diameter).
• Nanoemulsion stability was dependent on peptide concentration (1–4%), enzyme type, and storage temperature (4 °C vs. 25 °C).

Conclusions:

• Optimized WPI peptide size, enzyme type, and emulsification conditions can yield stable nanoemulsions.
• WPI-derived bioactive peptides demonstrate dual functionality as emulsifiers and bioactive compounds.
• This research highlights the potential of WPI peptides for developing functional nanoemulsions.