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What makes oil-in-water emulsions with pea protein stable?: The role of excess protein in network formation and yield stress development
Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - Ångström, Macromolecular Chemistry.
Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - Ångström, Macromolecular Chemistry.ORCID iD: 0000-0001-8185-3272
Univ Amsterdam, Van der Waals Zeeman Inst, Inst Phys, Sci Pk 904, NL-1018 XH Amsterdam, Netherlands..
2025 (English)In: Soft Matter, ISSN 1744-683X, E-ISSN 1744-6848, Vol. 21, no 19, p. 3757-3767Article in journal (Refereed) Published
Abstract [en]

Emulsions stabilized with pea protein exhibit enhanced stability only if excess protein is present in the continuous aqueous phase. We hypothesize that the additional protein, beyond the interfacial layer surrounding the oil droplets, is important for the emergence of a yield stress as well as for the overall stability and properties. Stable emulsions with oil concentrations of 40-60% v/v were prepared and compared to layers from various separated emulsions. Confocal microscopy visualized both the oil droplets and the protein distribution. Rheological measurements were used to assess mechanical properties and network formation. Small angle X-ray scattering provided quantitative structural information. Results identified that stable emulsions have a protein layer encapsulating the oil droplets and that excess protein forms irregular aggregates in the aqueous phase. Rheological analysis indicated that the protein aggregates contribute to network formation and give rise to a yield stress which enhances stability. Only for sufficiently high protein concentrations were the emulsions stable. Other samples separated and the upper phases were always similar in emulsion composition regardless of the initial component fractions. This study highlights the dual role of pea protein in emulsions as a dispersed protein network and as interfacial material. Determination of the most favourable emulsion composition provides insight into design of stable emulsions for applications.

Place, publisher, year, edition, pages
Royal Society of Chemistry, 2025. Vol. 21, no 19, p. 3757-3767
National Category
Physical Chemistry
Identifiers
URN: urn:nbn:se:uu:diva-566848DOI: 10.1039/d5sm00082cISI: 001468645500001PubMedID: 40241601OAI: oai:DiVA.org:uu-566848DiVA, id: diva2:1996371
Funder
EU, Horizon 2020, 956248Available from: 2025-09-09 Created: 2025-09-09 Last updated: 2026-02-19Bibliographically approved
In thesis
1. Droplet drama – physics of emulsions: How proteins hold it together
Open this publication in new window or tab >>Droplet drama – physics of emulsions: How proteins hold it together
2026 (English)Doctoral thesis, comprehensive summary (Other academic)
Abstract [en]

Protein-stabilized emulsions are used in many applications but their stabilization mechanisms, particularly for plant-based proteins, are only partially understood.  This dissertation investigates the structural and rheological properties of emulsions stabilized with pea proteins, focused on the role of the excess present in the continuous phase.  The main finding is that pea proteins contribute to the stability in two ways, both as a classical interfacial material that adsorbs to the oil-water interface, as well as being dispersed in the continuous phase where they form a hydrated fractal-like network.  This network increases viscosity and induces gelation, which provides great emulsion stability across a wide range of pH, compositions and temperatures.  

Systematic mapping of stable compositions revealed a previously unexplored stability region at intermediate oil concentrations (~ 10-60% v/v) and high protein concentrations (~ 5-15% w/v).  Structural characterization including confocal microscopy, and X-ray and neutron scattering, revealed that most of the protein is present in the continuous phase as hydrated aggregates forming networks that extend to micrometre length scales.  These networks are important for the resulting droplet size and rheological stability.  The emulsions exhibit shear thinning and thixotropic behaviour, typical of colloidal systems, as well as a yield stress that restricts droplet motion and contributes to stability.   The viscosity increases with protein concentration according to the Krieger Dougherty relationship when a large effective volume fraction of hydrated proteins is considered.  The droplet size decreases with increases of protein concentration, oil concentration, pH and applied shear, while changes of temperature have limited effect.  

Comparison with other emulsions formed with plant-based materials indicates that similar stabilization mechanisms may occur in those systems with sufficient excess biopolymer in the continuous phase.  This demonstrates the broader relevance of this work, where the formation of a viscoelastic network can significantly improve emulsion stability.  By introducing a new way of representing scattering data, rapid visual comparison between complex samples is simplified, which could improve efficiency in the handling of large data sets and aid automated interpretation with artificial intelligence.

Place, publisher, year, edition, pages
Uppsala: Acta Universitatis Upsaliensis, 2026. p. 98
Series
Digital Comprehensive Summaries of Uppsala Dissertations from the Faculty of Science and Technology, ISSN 1651-6214 ; 2643
Keywords
Pea protein, Emulsions, Scattering, SAXS, SANS, Contrast variation, Structural fingerprints, Rheology, Ternary phase map, Emulsion stability, Protein gel, Fractal network, Protein hydration, Food applications
National Category
Polymer Chemistry Physical Chemistry
Research subject
Chemistry with specialization in Macromolecular Chemistry
Identifiers
urn:nbn:se:uu:diva-579847 (URN)978-91-513-2749-5 (ISBN)
Public defence
2026-04-10, 10101, Siegbahnsalen, Ångströmlaboratoriet, Regementsvägen 10, Uppsala, 13:15 (English)
Opponent
Supervisors
Funder
EU, Horizon 2020, 956248
Available from: 2026-03-16 Created: 2026-02-19 Last updated: 2026-03-16

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Olsmats, EleonoraRennie, Adrian R.

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