Whey Protein Peptides have dual functions: Bioactivity and emulsifiers in oil-in-water nanoemulsion

Randy Adjonu, Gregory S. Doran, Peter Torley, Gilbert O. Sampson, Samson O. Agboola

Research output: Contribution to journalArticlepeer-review

Abstract

Whey protein isolate (WPI)-derived bioactive peptide fractions (1–3, 3–5, 5–10, 1–10, and >10 kDa) were for the first time used as emulsifiers in nanoemulsions. The formation and storage stability of WPI bioactive peptide-stabilized nanoemulsions depended on the peptide size, enzyme type, peptide concentration, and storage temperature. The highly bioactive <10 kDa fractions were either poorly surface-active or weak stabilizers in nanoemulsions. The moderately bioactive >10 kDa fractions formed stable nanoemulsions (diameter = 174–196 nm); however, their performance was dependent on the peptide concentration (1–4%) and enzyme type. Overall, nanoemulsions exhibited better storage stability (less droplet growth and creaming) when stored at lower (4 °C) than at higher (25 °C) temperatures. This study has shown that by optimizing peptide size using ultrafiltration, enzyme type and emulsification conditions (emulsifier concentration and storage conditions), stable nanoemulsions can be produced using WPI-derived bioactive peptides, demonstrating the dual-functionality of WPI peptides.

Original languageEnglish
Article number1812
JournalFoods
Volume11
Issue number12
DOIs
Publication statusPublished - 01 Jun 2022

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