Pulsed electric fields effects on the molecular structure and gelation of β-lactoglobulin concentrate and egg white

The structure modification of egg white proteins and β-lactoglobulin concentrate when subjected to long length pulses of high intensity electric fields (12.5 kV/cm) was evaluated and related to their sol–gel transition behavior. Both proteins were partially denatured (26–40%) when applying up to 10 pulses in the order of milliseconds. However, whilst the onset and peak, denaturation temperatures of the β-lactoglobulin concentrate were reduced by approximately 4–5 °C, the thermostability of egg white proteins was partially increased. Electrophoresis analysis revealed the formation of aggregates involving covalent bonds. The gelation rate of β-lactoglobulin concentrate was increased after the electric-treatment. In contrast, the gelation rate of egg white at 63 °C was lowered.