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From dairy to plant products: Understanding their structural fingerprints with X-rays
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
2025 (English)In: NPJ SCIENCE OF FOOD, ISSN 2396-8370, Vol. 9, no 1, article id 109Article in journal (Refereed) Published
Abstract [en]

Global interest in milk alternatives increases rapidly due to health awareness, their allergen-friendliness, and concerns about sustainability. While dairy product microstructure and rheology are widely studied, plant-based alternatives remain less understood, with limited comparative studies of different plant sources and brands. This study uses ultra-small, small and wide-angle X-ray scattering (USAXS, SAXS, WAXS) to analyse structural fingerprints of commercial plant-based milk, yoghurt and cream alternatives versus dairy products. These techniques allow characterization across multiple length scales from large oil droplets and aggregated structures to carbohydrate/protein networks and glyceride crystalline phases. Correlations between intensity and fat (USAXS) and carbohydrate content (SAXS) provide structural insights, while SAXS and WAXS data correlated with solid fat and crystal packing are important for melting behaviour and viscosity perception. Light scattering confirmed fat-content-related size trends and revealed larger structures of non-lipid materials in plant-based samples. The study provides a basis for understanding scattering data where structural fingerprint plots, using colour scales to compare intensity and intensity gradient, allow ready data interpretation that will be beneficial for analysis with artificial intelligence (AI) tools. This approach helps optimize plant-based formulations by connecting structure and functionality and demonstrates the potential of scattering techniques in food structure research and design.

Place, publisher, year, edition, pages
Springer Nature, 2025. Vol. 9, no 1, article id 109
National Category
Plant Biotechnology
Identifiers
URN: urn:nbn:se:uu:diva-563336DOI: 10.1038/s41538-025-00493-wISI: 001513747700003PubMedID: 40550822Scopus ID: 2-s2.0-105008824521OAI: oai:DiVA.org:uu-563336DiVA, id: diva2:1982498
Funder
EU, Horizon 2020, 956248Available from: 2025-07-08 Created: 2025-07-08 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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