Emulsifying peptides from potato protein predicted by bioinformatics: Stabilization of fish oil-in-water emulsions

Pedro J. García-Moreno*, Charlotte Jacobsen, Paolo Marcatili, Simon Gregersen Echers, Michael T. Overgaard, Mogens Larsen Andersen, Ann Dorit M. Sørensen, Egon Bech Hansen

*Corresponding author for this work

Research output: Contribution to journalJournal articleResearchpeer-review

45 Citations (Scopus)


This work investigated the use of bioinformatics to predict emulsifying peptides embedded in patatin proteins from potato (Solanum tuberosum). Six peptides (23–29 amino acids) with potentially different predominant structure at the oil/water interface (e.g. α-helix, β-strand or unordered) were identified within patatin sequences. The interfacial tension between peptides solutions and fish oil as well as the physical and oxidative stability of 5 wt% fish oil-in-water emulsions (pH 7) stabilized with synthetic predicted peptides were evaluated. The peptides predicted to have lower amphiphilic score (α1 and α2) led to emulsions with creaming after production and with low oxidative stability. On the other hand, a half hydrophobic and half hydrophilic peptide (γ1), which was predicted to have the highest amphiphilic score, showed a superior ability to reduce interfacial tension (even when compared to casein). γ1-Stabilized emulsion was physically stable during storage (48 h at 50 °C) and presented the lowest droplet size (D4,3 = 0.518 ± 0.011 μm). Electron spin resonance (ESR) and Oxygraph results indicated that the type of synthetic peptide used also affected the oxidative stability of fish oil-in-water emulsions differently. Therefore, this study shows the potential of using bioinformatics to predict emulsifying peptides, reducing time and cost of extensive screening hydrolysis processes.

Original languageEnglish
Article number105529
JournalFood Hydrocolloids
Publication statusPublished - Apr 2020


  • Electron spin resonance
  • Interfacial tension
  • Omega-3
  • Oxidative stability
  • Oxygraph
  • Physical stability


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