Volltext-Downloads (blau) und Frontdoor-Views (grau)

Formation of amyloid fibrils from ovalbumin under Ohmic heating

  • 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.

Download full text files

Export metadata

Additional Services

Search Google Scholar


Author:Eike JoeresORCiD, Stephan DruschORCiD, Stefan TöpflORCiD, Andreas JuadjurORCiD, Olympia Ekaterini PsathakiORCiD, Volker HeinzORCiD, Nino TerjungORCiD
Title (English):Formation of amyloid fibrils from ovalbumin under Ohmic heating
Parent Title (English):Heliyon
Document Type:Article
Year of Completion:2023
Release Date:2024/04/11
Tag:Amyloid fibril formation; Cross-beta sheet structures; Field flow fractioning; Moderate electric fields; Protein aggregation; Thioflavin T
Article Number:e22061
Page Number:13
Faculties:Fakultät AuL
DDC classes:600 Technik, Medizin, angewandte Wissenschaften / 610 Medizin, Gesundheit
Review Status:Veröffentlichte Fassung/Verlagsversion
Licence (German):License LogoCreative Commons - CC BY-NC-ND - Namensnennung - Nicht kommerziell - Keine Bearbeitungen 4.0 International