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Anthuparambil, Nimmi Das; Girelli, Anita; Timmermann, Sonja; Kowalski, Marvin; Akhundzadeh, Mohammad Sayed; Retzbach, Sebastian; Senft, Maximilian D.; Dargasz, Michelle; Gutmüller, Dennis; Hiremath, Anusha; Moron, Marc; Öztürk, Özgül; Poggemann, Hanna-Friederike; Ragulskaya, Anastasia; Begam, Nafisa; Tosson, Amir; Paulus, Michael; Westermeier, Fabian; Zhang, Fajun; Sprung, Michael; Schreiber, Frank; Gutt, Christian

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

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  • Media type: E-Article
  • Title: Exploring non-equilibrium processes and spatio-temporal scaling laws in heated egg yolk using coherent X-rays
  • Contributor: Anthuparambil, Nimmi Das; Girelli, Anita; Timmermann, Sonja; Kowalski, Marvin; Akhundzadeh, Mohammad Sayed; Retzbach, Sebastian; Senft, Maximilian D.; Dargasz, Michelle; Gutmüller, Dennis; Hiremath, Anusha; Moron, Marc; Öztürk, Özgül; Poggemann, Hanna-Friederike; Ragulskaya, Anastasia; Begam, Nafisa; Tosson, Amir; Paulus, Michael; Westermeier, Fabian; Zhang, Fajun; Sprung, Michael; Schreiber, Frank; Gutt, Christian
  • Published: Springer Science and Business Media LLC, 2023
  • Published in: Nature Communications, 14 (2023) 1
  • Language: English
  • DOI: 10.1038/s41467-023-41202-z
  • ISSN: 2041-1723
  • Origination:
  • Footnote:
  • Description: AbstractThe 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.
  • Access State: Open Access