Logo: to the web site of Uppsala University

uu.sePublications from Uppsala University
Change search
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf
Non-invasive multiscale characterization of protein networks and oil droplets in emulsions using spin-echo small angle neutron scattering
Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - Ångström, Macromolecular Chemistry.ORCID iD: 0009-0003-8175-2158
Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - Ångström, Macromolecular Chemistry.ORCID iD: 0000-0001-8185-3272
Show others and affiliations
2026 (English)In: Journal of Colloid and Interface Science, ISSN 0021-9797, E-ISSN 1095-7103, Vol. 711, article id 140071Article in journal (Refereed) Published
Abstract [en]

Hypothesis

Pea proteins can act not only as interfacial stabilizers of oil-in-water emulsions but also as gelling agents in the continuous phase. Protein gelation, rather than droplet jamming, may be the main mechanism of emulsion stability, providing a physical explanation for the creaminess of high-protein plant-based emulsions.

Experimental

Spin-echo small angle neutron scattering (SESANS) with D2O/H2O contrast variation was used to study 15% pea protein dispersions and emulsions with 40–60% rapeseed oil, 7.5% protein at pH 3 to 6.5. SESANS investigates length scales up to tens of micrometres, enabling simultaneous analysis of protein networks and oil droplets without dilution. Complementary small angle X-ray/neutron scattering were used to validate protein aggregate size, and hydration.

Findings

Protein dispersions at neutral pH formed mass fractal networks with small individual building blocks (radius ∼38 Å, hydration ∼70%). Emulsions consisted of oil droplets embedded in these networks, with droplet radii decreasing at higher oil fractions due to an effective higher protein concentration in the continuous phase, creating a denser network. Dispersions and emulsions at lower pH contained aggregated clusters of denatured proteins. These coarse and inhomogeneous networks gave increasing droplet radii at lower pH. Contrast variation enabled the separation of protein and oil droplet scattering, demonstrating that protein gelation rather than droplet jamming is the main mechanism of stability. This gives a physical explanation of the high viscosity of high-protein plant-based emulsions and is promising for these plant materials to be used as gelling agents in food applications.

Place, publisher, year, edition, pages
Elsevier, 2026. Vol. 711, article id 140071
Keywords [en]
Pea protein, Emulsion, Protein gel, Fractal network, Spin-echo small angle neutron scattering (SESANS), Contrast variation
National Category
Condensed Matter Physics Physical Chemistry
Identifiers
URN: urn:nbn:se:uu:diva-579228DOI: 10.1016/j.jcis.2026.140071OAI: oai:DiVA.org:uu-579228DiVA, id: diva2:2038402
Funder
EU, Horizon 2020, 956248Available from: 2026-02-13 Created: 2026-02-13 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

Open Access in DiVA

fulltext(5896 kB)29 downloads
File information
File name FULLTEXT01.pdfFile size 5896 kBChecksum SHA-512
9b907ba044ec235ddac607b7e86089c29aa9867ddbdb5d3adbbf2e6b0e5f00b1503dce684b6cb5ccf7da43d62d60e6ba691c9460641ab22c096362c2354d317a
Type fulltextMimetype application/pdf

Other links

Publisher's full text

Authority records

Olsmats, EleonoraRennie, Adrian R.

Search in DiVA

By author/editor
Olsmats, EleonoraRennie, Adrian R.
By organisation
Macromolecular Chemistry
In the same journal
Journal of Colloid and Interface Science
Condensed Matter PhysicsPhysical Chemistry

Search outside of DiVA

GoogleGoogle Scholar
The number of downloads is the sum of all downloads of full texts. It may include eg previous versions that are now no longer available

doi
urn-nbn

Altmetric score

doi
urn-nbn
Total: 1869 hits
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf