| Summary: | The thick fraction of egg white saturated with either N2O or Ar was irradiated in the dose range 1.5–45 kGy at 60Co gamma source. The gel structure decomposition and other processes accompanied with changes in protein molecular mass were followed by Sephadex G-200 exclusion chromatography, denaturing SDS-polyacrylamide gel electrophoresis, viscosity and turbidity measurements. The complex behaviour of viscosity was observed in the N2O saturated sample (where the hydrated electron was converted into the OH radical); the initial abrupt decrease that radually slows down reaching the minimum at 12 kGy (hmin = 2.7 mPa s) followed by the slow rise was measured. The Ar saturated sample ([eaq-] ~ [OH]) showed both the significantly faster initial decrease and lower viscosity minimum (hmin = 2.2 mPa s). The combined Sephadex G-200 exclusion chromatography and denaturing SDS-polyacrylamide gel electrophoresis data revealed that the three-dimensional egg white (hydrated) gel structure was (efficiently) decomposed even in the N2O saturated sample. The protein scission was detected in the entire dose range studied, while the protein agglomeration is not noticed at low doses (around 1.5 kGy); however, it dominates at higher doses. In the highest dose region studied, the loss of structure in SDS-PAGE chromatograms indicates that the agglomerates are formed from protein fragments rather than from intact proteins. The continuous linear increase in turbidity was measured. The results obtained indicate that ionizing radiation causes the breakdown of the protein network of the thick fraction of egg white via the reduction of S–S bridges by the hydrated electron and the protein fragmentation due to the direct action of ionizing radiation. The protein agglomeration is initiated by the reaction of the OH radical; its inefficiency at low doses is attributed to the glucose antioxidant properties and radical immobility.
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