TY  - JOUR
U1  - Wissenschaftlicher Artikel
A1  - Joeres, Eike
A1  - Drusch, Stephan
A1  - Töpfl, Stefan
A1  - Juadjur, Andreas
A1  - Psathaki, Olympia Ekaterini
A1  - Heinz, Volker
A1  - Terjung, Nino
T1  - Formation of amyloid fibrils from ovalbumin under Ohmic heating
JF  - Heliyon
N2  - Ohmic heating (OH) is an alternative sustainable heating technology that has demonstrated its potential to modify protein structures and aggregates. Furthermore, certain protein aggregates, namely amyloid fibrils (AF), are associated with an enhanced protein functionality, such as gelation. This study evaluates how Ohmic heating (OH) influences the formation of AF structures from ovalbumin source under two electric field strength levels, 8.5 to 10.5 and 24.0–31.0 V/cm, respectively. Hence, AF aggregate formation was assessed over holding times ranging from 30 to 1200 sunder various environmental conditions (3.45 and 67.95 mM NaCl, 80, 85 and 90 °C, pH = 7). AF were formed under all conditions. SDS-PAGE revealed that OH had a higher tendency to preserve native ovalbumin molecules. Furthermore, Congo Red and Thioflavin T stainings indicated that OH reduces the amount of AF structures. This finding was supported by FTIR measurements, which showed OH samples to contain lower amounts of beta-sheets. Field flow fractioning revealed smaller-sized aggregates or aggregate clusters occurred after OH treatment. In contrast, prolonged holding time or higher treatment temperatures increased ThT fluorescence, beta-sheet structures and aggregate as well as cluster sizes. Ionic strength was found to dominate the effects of electric field strength under different environmental conditions.
KW  - Moderate electric fields
KW  - Amyloid fibril formation
KW  - Protein aggregation
KW  - Thioflavin T
KW  - Field flow fractioning
KW  - Cross-beta sheet structures
Y1  - 2023
UN  - https://nbn-resolving.org/urn:nbn:de:bsz:959-opus-58102
SN  - 2405-8440
SS  - 2405-8440
U6  - https://doi.org/10.1016/j.heliyon.2023.e22061
DO  - https://doi.org/10.1016/j.heliyon.2023.e22061
VL  - 9
IS  - 11
SP  - 13
S1  - 13
ER  -