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Understanding Stabilization of Oil-in-Water Emulsions with Pea Protein – Studies of Structure and Properties
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
2024 (English)In: Langmuir, ISSN 0743-7463, E-ISSN 1520-5827, Vol. 40, no 26, p. 13386-13396Article in journal (Refereed) Published
Abstract [en]

This study investigates the stability and structure of oil-in-water emulsions stabilized by pea protein. Of the wide range of emulsion compositions explored, a region of stability at a minimum of 5% w/v pea protein and 30-50% v/v oil was determined. This pea protein concentration is more than what is needed to form a layer covering the interface. X-ray scattering revealed a thick, dense protein layer at the interface as well as hydrated protein dispersed in the continuous phase. Shear-thinning behavior was observed, and the high viscosity in combination with the thick protein layer at the interface creates a good stability against creaming and coalescence. Emulsions in a pH range from acidic to neutral were studied, and the overall stability was observed to be broadly similar independently of pH. Size measurements revealed polydisperse protein particles. The emulsion droplets are also very polydisperse. Apart from understanding pea protein-stabilized emulsions in particular, insights are gained about protein stabilization in general. Knowledge of the location and the role of the different components in the pea protein material suggests that properties such as viscosity and stability can be tailored for various applications, including food and nutraceutical products.

Place, publisher, year, edition, pages
American Chemical Society (ACS), 2024. Vol. 40, no 26, p. 13386-13396
National Category
Physical Chemistry Circular Food Process Technologies Food Biotechnology
Identifiers
URN: urn:nbn:se:uu:diva-540062DOI: 10.1021/acs.langmuir.4c00540ISI: 001252900900001PubMedID: 38904703OAI: oai:DiVA.org:uu-540062DiVA, id: diva2:1905156
Funder
EU, Horizon 2020, 956248Available from: 2024-10-11 Created: 2024-10-11 Last updated: 2026-02-25Bibliographically 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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