Effect of Acetylation of Ovalbumin on Its Adsorption Behavior at Solid/Liquid Interface | Zendy

A. Bhaduri | Zendy; Naotoshi Matsudomi | Zendy; K. P. Das | Zendy

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Effect of Acetylation of Ovalbumin on Its Adsorption Behavior at Solid/Liquid Interface

Author(s) -

A. Bhaduri,

Naotoshi Matsudomi,

K. P. Das

Publication year - 1996

Publication title -

bioscience biotechnology and biochemistry

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.509

H-Index - 116

eISSN - 1347-6947

pISSN - 0916-8451

DOI - 10.1271/bbb.60.1559

Subject(s) - ovalbumin , adsorption , acetylation , lysine , chemistry , chemical engineering , organic chemistry , biochemistry , antigen , amino acid , biology , genetics , gene , engineering

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.

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