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Emulsions stabilized by pea protein – Hydration and protein distribution
Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - Ångström, Macromolecular Chemistry.ORCID iD: 0009-0003-8175-2158
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2025 (English)In: Food Hydrocolloids, ISSN 0268-005X, E-ISSN 1873-7137, Vol. 162, article id 110989Article in journal (Refereed) Published
Abstract [en]

This study investigates the structural properties of oil-in-water emulsions stabilized with pea protein using small-angle neutron scattering (SANS) and small-angle X-ray scattering (SAXS) techniques particularly as regards the hydration of the protein. The high protein content needed for stability (>5% w/v) is identified as being present mainly as a dispersed component in the aqueous phase contributing to network formation and increased viscosity. The hydration of the protein was distinguished through measurements with various D2O/H2O ratios. The dispersed protein is highly hydrated (75–80% water content). Additionally, pH-dependent scattering studies revealed significant structural rearrangements and aggregation of pea protein at acidic pH and around the isoelectric point, without greatly impacting emulsion stability. A range of pea protein concentrations were studied with increased amount of dispersed material in the aqueous phase at higher protein concentrations that results in smaller oil droplets and enhanced emulsion stability. Overall, these findings highlight the complex interplay between protein hydration, pH-induced changes and aggregation, and concentration on emulsion stability. This provides insights for optimizing protein-based emulsions in food applications, paving the way for novel protein-based emulsifiers.

Place, publisher, year, edition, pages
Elsevier, 2025. Vol. 162, article id 110989
National Category
Condensed Matter Physics
Research subject
Chemistry with specialization in Macromolecular Chemistry
Identifiers
URN: urn:nbn:se:uu:diva-546546DOI: 10.1016/j.foodhyd.2024.110989ISI: 001405025900001Scopus ID: 2-s2.0-85213083948OAI: oai:DiVA.org:uu-546546DiVA, id: diva2:1925950
Funder
EU, Horizon 2020Available from: 2025-01-09 Created: 2025-01-09 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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