ArticleNature communications2023
Exploring non-equilibrium processes and spatio-temporal scaling laws in heated egg yolk using coherent X-rays.
Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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Who cites it
6 citing papers in PubMed, 13 citations in OpenAlex.
- A pipeline for megahertz X-ray photon correlation spectroscopy on soft matter samples at the MID instrument of European XFEL.Journal of synchrotron radiation · 2026Article
- Food-Grade Emulsion Gels as Nutrient Delivery Systems-Standardized Workflow for Fabrication, Characterization, and Application.Gels (Basel, Switzerland) · 2026Review
- Universal progression of structure and dynamics in colloidal nanocrystal gels during salt-accelerated aging.Science advances · 2026Article
- Potential Anti-Aging Effects of a Dietary Supplement From the Algal-Derived Omega-3 DHA in Aged SAMP 8 Mice.Food science & nutrition · 2026Article
- Coherent X-rays reveal anomalous molecular diffusion and cage effects in crowded protein solutions.Nature communications · 2025Article
- Exploring TEM Coherence Properties via Speckle Contrast Analysis in Coherent Electron Scattering of Amorphous Material.Nanomaterials (Basel, Switzerland) · 2023Article
Corrections and comments
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Authors and funding
22 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The soft-grainy microstructure of cooked egg yolk is the result of a series of out-of-equilibrium processes of its protein-lipid contents; however, it is unclear how egg yolk constituents contribute to these processes to create the desired microstructure. By employing X-ray photon correlation spectroscopy, we investigate the functional contribution of egg yolk constituents: proteins, low-density lipoproteins (LDLs), and yolk-granules to the development of grainy-gel microstructure and microscopic dynamics during cooking. We find that the viscosity of the heated egg yolk is solely determined by the degree of protein gelation, whereas the grainy-gel microstructure is controlled by the extent of LDL aggregation. Overall, protein denaturation-aggregation-gelation and LDL-aggregation follows Arrhenius-type time-temperature superposition (TTS), indicating an identical mechanism with a temperature-dependent reaction rate. However, above 75 °C TTS breaks down and temperature-independent gelation dynamics is observed, demonstrating that the temperature can no longer accelerate certain non-equilibrium processes above a threshold value.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the Socratic graph.