Effect of acetylation of ovalbumin on its adsorption behavior at solid/liquid interface.
This paper reports the effect of modification of lysine residues on the adsorption of ovalbumin at alumina/water interface. It has been shown that the pH dependence of the adsorption changes on acetylation of lysine. Thus at pH 7.6 acetylated ovalbumin does not show any affinity for alumina surface although unmodified protein does. It seems that although electrostatic interactions are operative, surface unfolding of proteins and surface hydrophobicity of protein also control the adsorption of ovalbumin onto alumina.
Bhaduri
A
A
Department of Chemistry, Bose Institute, Calcutta, India.
Matsudomi
N
N
Das
K P
KP
D000107:Acetylation; D000327:Adsorption; D000537:Aluminum Oxide / Q000737:chemistry*; D006863:Hydrogen-Ion Concentration; D016014:Linear Models; D008239:Lysine / Q000737:chemistry*; D009994:Osmolar Concentration; D010047:Ovalbumin / Q000737:chemistry*; D012995:Solubility; D055672:Static Electricity; D014867:Water / Q000737:chemistry*
D014867:Water; D010047:Ovalbumin; D008239:Lysine; D000537:Aluminum Oxide