To Investigate the Effect of Salt Concentration on Ovalbumin Aggregation

Abstract

In this work, we investigated the fibrillation of a 44.5 KDa egg white glycoprotein, Ovalbumin, as a function of salt (NaCl) concentration using intrinsic (Tryptophan) and extrinsic (ANS and ThT) fluorophores. The conformational changes were monitored by using Fluorescence and CD spectroscopic techniques. Both the studies indicate that there is an increase in β-sheet and decrease in α-helix content of the protein as the concentration of salt increases, indicating unfolding of protein. This finding demonstrates that aggregation of Ovalbumin is induced by the salt.