Radiation-induced cross-linking and scissoring of proteins in egg white

• Published in: Radiation physics and chemistry (1993) Vol. 47; no. 3; pp. 445 - 447
• Main Authors: JOSIMOVIC, L. J, RADOJCIC, M, MILOSAVLJEVIC, B. H
• Format: Journal Article Conference Proceeding
• Language: English
• Published: Oxford Elsevier Ltd 01-03-1996; Elsevier
• Subjects: Applied sciences; Crosslinking and degradation; Exact sciences and technology; Physicochemistry of polymers; Polymers and radiations; Radiation resistance; Radiation dose; Gamma radiation; Animal protein; Radiochemical degradation; Egg white; Experimental study; Radiochemical crosslinking
• ISSN: 0969-806X; 1879-0895
• DOI: 10.1016/0969-806X(95)00139-O

Two kinds of radiation-induced protein damages, cross-linking and scissoring, were studied using a thin fraction of avian egg white. It was found that at a dose of 10 kGy in N
2O saturated samples only one third of the affected protein molecules underwent aggregation, while, contrary to the results obtained with diluted protein solutions, the rest took part in the fragmentation reaction. The fragments obtained had a uniform molecular weight distribution. The overall
G-value was found to be 0.25. In air saturated samples the scissoring dominated ten times over cross-linking with the fragments of discrete and well resolved molecular weights. The overall
G-value was equal to 0.3. Both
G-values are three times smaller than the corresponding values obtained in the experiments with denatured and purified proteins. The egg white radiation stability was found to be, at least in part, due to the presence of glucose which, in turn, acts as an antioxidant. Other relevant factors which may affect the radiation chemistry of the egg white protein composite are also discussed.