Self Crowding as a Determinant of egg white Photostability

Aqueous suspensions containing increasing amounts (0.1-200 g/L) of egg white at different ionic strength (0.025-1.000 M NaCl) were characterised for critical concentration associated to self crowding phenomena. Samples were then exposed to 30 W m− 2 UV-C light for 10 min. Self crowded proteins resulted fully resistant to photodegradation. In uncrowded conditions, egg white underwent fragmentation and aggregation. The increase in ionic strength favoured protein folding. Compact proteins were more prone to intramolecular rearrangement and reached photostability at higher concentrations. Self crowding could be selectively exploited to steer protein resistance to physical stresses.