EFFECT OF ACETYLATION OF OVALBUMIN ON ITS ADSORPTION BEHAVIOR AT SOLID LIQUID INTERFACE/

This paper reports the effect of modification of lysine residues on th e adsorption of ovalbumin at alumina/water interface, It has been show n that the pH dependence of the adsorption changes on acetylation of l ysine, Thus at pH 7.6 acetylated ovalbumin does not show any affinity for alumina surface although unmodified protein does, It seems that al though electrostatic interactions are operative, surface unfolding of proteins and surface hydrophobicity of protein also control the adsorp tion of ovalbumin onto alumina.