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Salt induced slowdown of kinetics and dynamics during thermal gelation of egg-yolk.
Anthuparambil, Nimmi Das; Timmermann, Sonja; Dargasz, Michelle; Retzbach, Sebastian; Senft, Maximilian D; Begam, Nafisa; Ragulskaya, Anastasia; Paulus, Michael; Zhang, Fajun; Westermeier, Fabian; Sprung, Michael; Schreiber, Frank; Gutt, Christian.
Afiliación
  • Anthuparambil ND; Department Physik, Universität Siegen, 57072 Siegen, Germany.
  • Timmermann S; Department Physik, Universität Siegen, 57072 Siegen, Germany.
  • Dargasz M; Department Physik, Universität Siegen, 57072 Siegen, Germany.
  • Retzbach S; Institut für Angewandte Physik, Universität Tübingen, 72076 Tübingen, Germany.
  • Senft MD; Institut für Angewandte Physik, Universität Tübingen, 72076 Tübingen, Germany.
  • Begam N; Institut für Angewandte Physik, Universität Tübingen, 72076 Tübingen, Germany.
  • Ragulskaya A; Department of Physics, Banaras Hindu University, Varanasi 221005, India.
  • Paulus M; Institut für Angewandte Physik, Universität Tübingen, 72076 Tübingen, Germany.
  • Zhang F; Fakultät Physik/DELTA, Technische Universität Dortmund, 44221 Dortmund, Germany.
  • Westermeier F; Institut für Angewandte Physik, Universität Tübingen, 72076 Tübingen, Germany.
  • Sprung M; Deutsches Elektronen-Synchrotron DESY, 22607 Hamburg, Germany.
  • Schreiber F; Deutsches Elektronen-Synchrotron DESY, 22607 Hamburg, Germany.
  • Gutt C; Institut für Angewandte Physik, Universität Tübingen, 72076 Tübingen, Germany.
J Chem Phys ; 161(5)2024 Aug 07.
Article en En | MEDLINE | ID: mdl-39105556
ABSTRACT
We investigated the effect of the NaCl concentration (0.3-2M) on the structure and dynamics of hen egg yolk at room temperature and during thermal gelation at temperatures in the range of 66-90 °C utilizing low-dose x-ray photon correlation spectroscopy in ultra-small angle x-ray scattering geometry. With an increase in the salt concentration, we observe progressive structural and dynamic changes at room temperature, indicating the disruption of yolk components such as yolk-granules and yolk-plasma proteins. Temperature- and salt-dependent structural and dynamic investigations suggest a delay in the gel formation and aggregation of yolk low-density lipoproteins with increasing ionic strength. However, the time-temperature superposition relationship observed in all samples suggests an identical mechanism underlying protein aggregation-gelation with a temperature-dependent reaction rate. The sol-gel transition time extracted from kinetic and dynamic information follows Arrhenius's behavior, and the activation energy (460 kJ/mol) is found to be independent of the salt concentration.

Texto completo: 1 Base de datos: MEDLINE Idioma: En Revista: J Chem Phys Año: 2024 Tipo del documento: Article

Texto completo: 1 Base de datos: MEDLINE Idioma: En Revista: J Chem Phys Año: 2024 Tipo del documento: Article