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On the Emulsifying Properties of Self-Assembled Pea Protein Particles
Simha Sridharan1,2, Marcel B J Meinders3, Johannes H Bitter1
1Biobased Chemistry and Technology (BCT), Wageningen University and Research, Bornse Weilanden 9, 6708 WG, Wageningen, The Netherlands.
Langmuir : the ACS Journal of Surfaces and Colloids
|September 29, 2020
Summary
Pea protein molecules, not particles, are the main emulsifiers for oil-in-water emulsions at pH 3. This finding clarifies the stabilization mechanism for acidic food systems.
Area of Science:
- Food Science
- Protein Chemistry
- Colloid Science
Background:
- Pea proteins function as oil-in-water emulsifiers under neutral and acidic conditions.
- Acidic conditions cause pea proteins to form submicrometer particles, previously thought to stabilize emulsions via a Pickering mechanism.
Purpose of the Study:
- To determine whether pea protein particles or molecules are the primary emulsifying agents at pH 3.
- To re-evaluate the emulsion stabilization mechanism of pea proteins in acidic environments.
Main Methods:
- Comparison of theoretical and experimental surface load on oil droplets.
- Emulsification experiments using pea protein molecules after removing protein particles.
Main Results:
- Pea protein particles could only cover 3.2% of the oil droplet surface, insufficient for stabilization.
- Pea protein molecules covered 47% of the oil droplet surface, indicating a significant stabilizing role.
- Experiments with only protein molecules confirmed their primary role in emulsion stabilization.
Conclusions:
- Pea protein molecules, not particles, are the predominant stabilizers of oil-in-water emulsions at pH 3.
- This research clarifies the emulsion stabilization mechanism of pea proteins in acidic conditions, challenging previous assumptions.
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