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Exploring non-equilibrium processes and spatio-temporal scaling laws in heated egg yolk using coherent X-rays

Author

Listed:
  • Nimmi Das Anthuparambil

    (Deutsches Elektronen-Synchrotron DESY
    Universität Siegen)

  • Anita Girelli

    (Universität Tübingen)

  • Sonja Timmermann

    (Universität Siegen)

  • Marvin Kowalski

    (Universität Siegen)

  • Mohammad Sayed Akhundzadeh

    (Universität Siegen)

  • Sebastian Retzbach

    (Universität Tübingen)

  • Maximilian D. Senft

    (Universität Tübingen)

  • Michelle Dargasz

    (Universität Siegen)

  • Dennis Gutmüller

    (Universität Tübingen)

  • Anusha Hiremath

    (Universität Tübingen)

  • Marc Moron

    (Technische Universität Dortmund)

  • Özgül Öztürk

    (Universität Siegen)

  • Hanna-Friederike Poggemann

    (Universität Tübingen)

  • Anastasia Ragulskaya

    (Universität Tübingen)

  • Nafisa Begam

    (Universität Tübingen)

  • Amir Tosson

    (Universität Siegen)

  • Michael Paulus

    (Technische Universität Dortmund)

  • Fabian Westermeier

    (Deutsches Elektronen-Synchrotron DESY)

  • Fajun Zhang

    (Universität Tübingen)

  • Michael Sprung

    (Deutsches Elektronen-Synchrotron DESY)

  • Frank Schreiber

    (Universität Tübingen)

  • Christian Gutt

    (Universität Siegen)

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.

Suggested Citation

  • Nimmi Das Anthuparambil & Anita Girelli & Sonja Timmermann & Marvin Kowalski & Mohammad Sayed Akhundzadeh & Sebastian Retzbach & Maximilian D. Senft & Michelle Dargasz & Dennis Gutmüller & Anusha Hire, 2023. "Exploring non-equilibrium processes and spatio-temporal scaling laws in heated egg yolk using coherent X-rays," Nature Communications, Nature, vol. 14(1), pages 1-12, December.
    • Handle: RePEc:nat:natcom:v:14:y:2023:i:1:d:10.1038_s41467-023-41202-z
    DOI: 10.1038/s41467-023-41202-z
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    References listed on IDEAS

    as
    1. Mario Reiser & Anita Girelli & Anastasia Ragulskaya & Sudipta Das & Sharon Berkowicz & Maddalena Bin & Marjorie Ladd-Parada & Mariia Filianina & Hanna-Friederike Poggemann & Nafisa Begam & Mohammad Sa, 2022. "Resolving molecular diffusion and aggregation of antibody proteins with megahertz X-ray free-electron laser pulses," Nature Communications, Nature, vol. 13(1), pages 1-10, December.
    2. Amlan Das & Peter M. Derlet & Chaoyang Liu & Eric M. Dufresne & Robert Maaß, 2019. "Stress breaks universal aging behavior in a metallic glass," Nature Communications, Nature, vol. 10(1), pages 1-9, December.
    3. Kresten Lindorff-Larsen & Robert B. Best & Mark A. DePristo & Christopher M. Dobson & Michele Vendruscolo, 2005. "Simultaneous determination of protein structure and dynamics," Nature, Nature, vol. 433(7022), pages 128-132, January.
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