Dynamic Interfacial Architectures: Cruciferin‐Stabilized Oil/Water Interfaces for Sustainable Emulsions

Holderer, Olaf; Landman, Jasper; Kohlbrecher, Joachim; Wu, Baohu; Zolnierczuk, Piotr; Müller, Maren; Frielinghaus, Henrich; Förster, Stephan; Schwärzer, Kuno; Sagis, Leonard; Shen, Penghui; Yang, Jack; Heiden‐Hecht, Theresia

doi:10.1002/admi.202500368

Title: Dynamic Interfacial Architectures: Cruciferin‐Stabilized Oil/Water Interfaces for Sustainable Emulsions

Journal Article · Thu Aug 07 00:00:00 UTC 2025 · Advanced Materials Interfaces

DOI: https://doi.org/10.1002/admi.202500368 · OSTI ID:2586825

Holderer, Olaf ^[1]; Landman, Jasper ^[2]; Kohlbrecher, Joachim ^[3]; Wu, Baohu ^[1];

^[4]; Müller, Maren ^[1]; Frielinghaus, Henrich ^[1]; Förster, Stephan ^[1]; Schwärzer, Kuno ^[1]; Sagis, Leonard ^[2]; Shen, Penghui ^[2]; Yang, Jack ^[2];

^[1]

Juelich Centre for Neutron Science (JCNS) at Heinz Maier-Leibnitz Zentrum (MLZ), Forschungszentrum Juelich GmbH, Garching (Germany)
Wageningen Univ. (Netherlands)
Paul Scherrer Inst. (PSI), Villigen (Switzerland)
Oak Ridge National Laboratory (ORNL), Oak Ridge, TN (United States)

Stabilizing oil-water interfaces in emulsions by plant-based proteins provides sustainable and tunable ways for designing emulsions with specific properties, for food, healthcare, and pharmaceuticals. Cruciferin, a protein from rapeseed, has great potential as green emulsifier, but details about its structure and mobility at oil-water interfaces are largely unknown. Here, these properties are studied with small angle neutron and x-ray scattering, and neutron spin echo spectroscopy, analyzed by atomistic modelling of scattering curves and coarse-grained modelling, to gain insight into interface coverage, and molecular conformation and mobility at the interface. Cruciferin assumes trimeric conformations at the interface, as in solution, but with its protrusions from the central core of the subunits (“arms”) more compressed. Interfacial mobility is only marginally lower than in solution, indicating the arms still transiently extend and preserve a network, for the first time revealing the mechanism how cruciferin forms highly elastic 2d gel-like oil-water interfaces, as observed in macroscopic rheology. The high interfacial mobility may help in self-repairing non-stabilized interfacial fractions, reducing coalescence. These findings provide a deeper molecular level understanding of proteins at oil-water interfaces, which can stimulate development of new plant-based emulsion products, and contribute to the global protein transition.

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Research Organization:: Oak Ridge National Laboratory (ORNL), Oak Ridge, TN (United States)

Sponsoring Organization:: USDOE Office of Science (SC), Basic Energy Sciences (BES). Scientific User Facilities (SUF)

Grant/Contract Number:: AC05-00OR22725

OSTI ID:: 2586825

Journal Information:: Advanced Materials Interfaces, Journal Name: Advanced Materials Interfaces Journal Issue: 17 Vol. 12; ISSN 2196-7350

Publisher:: WileyCopyright Statement

Country of Publication:: United States

Language:: English

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