3D structure of protein networks and lipid globules in heat-treated egg yolk revealed by X-ray holo-tomography
Upon heating, egg yolk transforms from a liquid to a grainy gel due to a combination of lipid aggregation, protein denaturation–aggregation–gelation and other processes. This heat-induced solidification of egg yolk can serve as a useful model system for the investigation of protein denaturation and gelation in biological systems in general. Using X-ray holographic tomography, we studied the heat-induced changes in egg yolk on the micron to sub-micron length scale. In contrast to electron microscopy, X-ray holography does not require sample staining, fixation, or drying, which potentially alter the sample and harm sample fidelity. Our results reveal a developing separation between proteins and lipids with fatty components rapidly aggregating into large globules around 40 μ m in diameter. • X-ray holo-tomography offers 3D resolution better than 0.5 μ m for soft biosamples. • Heating egg yolk causes growing separation between proteins and lipids. • Fatty components in cooked egg yolk rapidly aggregate into 40 μ m large globules.
Authors
- Nimmi Das Anthuparambil (ORCID: https://orcid.org/0000-0001-5338-2004)
- Frederik Unger (ORCID: https://orcid.org/0000-0002-7127-3829)
- Rekha Gautam (ORCID: https://orcid.org/0000-0002-1176-8491)
- Silja Flenner (ORCID: https://orcid.org/0000-0002-2951-2304)
- Peter Modregger (ORCID: https://orcid.org/0000-0002-2648-6403)
- Imke Greving (ORCID: https://orcid.org/0000-0002-6231-1088)
- Christian Gutt (ORCID: https://orcid.org/0000-0002-0051-8542)
- Felix Wittwer (ORCID: https://orcid.org/0000-0002-5050-1669)
Institutions
- University of Siegen (DE)
- Folkwang University of the Arts (DE)
- Deutsches Elektronen-Synchrotron DESY (DE)
- Helmholtz-Zentrum Hereon (DE)
Publication Details
- Journal
- Journal of Food Engineering
- Published
- 2025-12-12
- DOI
- https://doi.org/10.1016/j.jfoodeng.2025.112916
- Primary Topic
- Proteins in Food Systems
- Type
- article
- Field-Weighted Citation Impact
- 0.00