Open Access

Eike Joeres, Henry Schölzel, Stephan Drusch, Stefan Töpfl, Volker Heinz, Nino Terjung

• The present study investigates properties of heat-induced, self-standing gels of globular proteins. Native egg white protein (EWP) with 9,8 wt% protein and 0,395 wt% NaCl content was adjusted to pH = 7,0 and heated from 25 to 85 °C via Ohmic heating (OH) and conventional heating (COV) with respective come-up times (CUT, 240 and 1200 s) and holding times (HOLD, 30 and 900 s). Gels heated under OH showed lower denaturation levels and less water holding capacity. When HOLD was short, the firmness of OH gels exceeded COV gel firmness but deceeded at long HOLD. Similarly, at short HOLD OH samples presented higher hydrophobic interactions whereas at long HOLD COV gels showed more hydrophobic interactions. This correlated with changes of intermolecular beta-sheet structures which increased with HOLD at COV but decreased or remained unchanged during OH. Furthermore, as an SDS-PAGE revealed the main EWP, ovalbumin, did not fully denature when heated via OH, this lead to the assumption that the oscillatory electric field partially interferes the complete denaturation and development of intermolecular beta-sheet structures and hydrophobic interactions during thermal gelation of this protein. Scanning electron microscopy also showed deviances in network structures between OH and COV as COV gels exhibited a denser and OH gels a more open and porous network structure.