Effects of microviscosity, dry electron scavenging, and protein mobility on the radiolysis of albumen hydrogel.

Nanosecond pulse radiolysis experiments performed on the oxygen and nitrogen saturated thick fraction of egg white (which has an immeasurably high macroviscosity) produced a rate constant for hydrated electron reaction with oxygen equal to 1.7 × 10(10) M(-1) s(-1) at 18 °C, indicating that, due to the very low microviscosity, hydrated electrons are as mobile and reactive in the albumen hydrogel as in neat water. Also, the radiolytic yield for the hydrated electron (G-value) in the thick fraction of egg white (measured at the end of a 14 ns electron pulse) was found to be 86% of that determined in neat water, which can be attributed to the reaction of dry electrons with the protein constituents. Steady-state γ radiolysis studies on air-saturated thick and thin fraction (true solution) revealed that the immobility of egg white proteins disfavors reactions that result in molecular mass change.