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Protein Fibrils Induce Emulsion Stabilization.

Jinfeng Peng1, Joana Ralfas Simon1, Paul Venema1

  • 1Laboratory of Physics and Physical Chemistry of Foods, Department of Agrotechnology and Food Sciences, Wageningen University , P.O. Box 17, 6700 AA, Wageningen, The Netherlands.

Langmuir : the ACS Journal of Surfaces and Colloids
|February 17, 2016
PubMed
Summary
This summary is machine-generated.

Protein fibrils influence oil-in-water emulsions, causing aggregation at low concentrations and stabilization at high concentrations. This aggregation is reversible upon dilution, indicating kinetic stabilization.

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Area of Science:

  • Colloid and Surface Science
  • Biophysical Chemistry
  • Materials Science

Background:

  • Protein fibrils are increasingly used as stabilizers or structuring agents in food and cosmetic emulsions.
  • Understanding their interaction with emulsion droplets is crucial for controlling emulsion properties.

Purpose of the Study:

  • To investigate the effect of protein fibril concentration on the behavior of oil-in-water emulsions.
  • To elucidate the mechanisms governing emulsion stabilization or destabilization by protein fibrils.

Main Methods:

  • Rheology was employed to measure emulsion viscosity and viscoelastic properties.
  • Diffusing wave spectroscopy (DWS) was used to probe droplet dynamics and aggregation.
  • Confocal laser scanning microscopy (CLSM) provided visual evidence of droplet arrangements and fibril distribution.

Main Results:

  • Depletion flocculation and enhanced creaming were observed above a minimum fibril concentration.
  • At higher fibril concentrations, emulsions became stabilized with smaller, concentration-independent droplet aggregates.
  • Droplet aggregation was reversible upon dilution with pH 2 HCl or fibril solution.

Conclusions:

  • Protein fibrils can induce both destabilization (flocculation) and stabilization of oil-in-water emulsions depending on their concentration.
  • The stabilization at high fibril concentrations is attributed to kinetic stabilization, not network formation.
  • The reversible nature of aggregation suggests potential for controlled emulsion formulation and processing.