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@ARTICLE{Anthuparambil:573576,
author = {Anthuparambil, Nimmi das and Girelli, Anita and Timmermann,
Sonja and Kowalski, Marvin and Akhundzadeh, Mohammad Sayed
and Retzbach, Sebastian and Senft, Maximilian and Dargasz,
Michelle and Gutmueller, Dennis and Hiremath, Anusha and
Moron, Marc and Öztürk, Özgül and Poggemann,
Hanna-Friederike and Ragulskaya, Anastasia and Begam, Nafisa
and Tosson, Amir and Paulus, Michael and Westermeier, Fabian
and Zhang, Fajun and Sprung, Michael and Schreiber, Frank
and Gutt, Christian},
title = {{E}xploring non-equilibrium processes and spatio-temporal
scaling laws in heated egg yolk using coherent {X}-rays},
journal = {Nature Communications},
volume = {14},
issn = {2041-1723},
address = {[London]},
publisher = {Nature Publishing Group UK},
reportid = {PUBDB-2023-00861},
pages = {5580},
year = {2023},
note = {Beamtime was allocated for FS proposals II-20210008 and
II-20211600. The authors also thank the support of DFG (NFDI
40/1), BMBF (05K19PS1, 05K20PSa, 05K22PS1, 05K20VTA), and
NFDI for this work.},
abstract = {The soft-grainy texture of cooked egg yolk is the result of
a series of out-of-equilibrium processes of its
protein-lipid contents; however, it is unclearhow egg yolk
constituents contribute to these processes to create the
desiredtexture. By employing X-ray photon correlation
spectroscopy, we investigatethe functional contribution of
egg yolk constituents: proteins, low-densitylipoproteins
(LDLs), and yolk-granules to the development of
grainy-gelmicrostructure and microscopic dynamics during
cooking. We find that theviscosity of the heated egg yolk is
solely determined by the degree ofprotein gelation, whereas
the grainy-gel texture is controlled by the extent of LDL
aggregation. Overall, protein
denaturation-aggregation-gelation andLDL-aggregation follows
Arrhenius-type time-temperature superposition
(TTS),indicating an identical reaction route with a
temperature-dependent reactionrate. However, above 75 ◦C
TTS breaks down and temperature-independentgelation dynamics
is observed, demonstrating that the temperature can nolonger
accelerate certain non-equilibrium processes above a
threshold value.},
cin = {FS-PETRA-S / DOOR ; HAS-User},
ddc = {500},
cid = {I:(DE-H253)FS-PETRA-S-20210408 /
I:(DE-H253)HAS-User-20120731},
pnm = {633 - Life Sciences – Building Blocks of Life: Structure
and Function (POF4-633) / 6G3 - PETRA III (DESY) (POF4-6G3)
/ 05K19PS1 - Instrumentierung, um die Dynamik von
biologischen Proben mit Korrelationsspektroskopie zu messen.
(BMBF-05K19PS1) / 05K20PSA - Verbundprojekt 05K2020 -
2019-06075 Protein-Dyn: Dynamik von Proteinen in Lösungen
auf multiplen Längen und Zeitskalen (Teilprojekt 1)
(BMBF-05K20PSA) / 05K20VTA - Verbundprojekt 05K2020 -
2019-06075 Protein-Dyn: Dynamik von Proteinen in Lösungen
auf multiplen Längen und Zeitskalen (Teilprojekt 2)
(BMBF-05K20VTA) / 05K22PS1 - Schnelle
Korrelationsspektroskopie an der ESRF-EBS (BMBF-05K22PS1) /
DFG project 390677874 - EXC 2033: RESOLV (Ruhr Explores
Solvation) (390677874)},
pid = {G:(DE-HGF)POF4-633 / G:(DE-HGF)POF4-6G3 /
G:(DE-Ds200)BMBF-05K19PS1 / G:(DE-Ds200)BMBF-05K20PSA /
G:(DE-Ds200)BMBF-05K20VTA / G:(DE-Ds200)BMBF-05K22PS1 /
G:(GEPRIS)390677874},
experiment = {EXP:(DE-H253)P-P10-20150101},
typ = {PUB:(DE-HGF)16},
pubmed = {37696830},
UT = {WOS:001157889300011},
doi = {10.1038/s41467-023-41202-z},
url = {https://bib-pubdb1.desy.de/record/573576},
}