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1986•Journal of the American Oil Chemists SocietyRequires access

The Ionic Modification of the Surface Charge and Isoelectric Point of Soy Protein

W. S. Chen, William G. Soucie

Open publisher page 21 citations

Abstract

Abstract The effect of anionic and cationic binding on the surface charge of soy proteins was measured by electrokinetic analysis. All of the ions investigated suppressed the surface charge of the protein; however, certain multivalent ions such as Al (III), Fe (III), hexametaphosphate and tripolyphosphate also altered the isoelectric point of the protein. The results indicated the unpredictability of ionic effects on protein functionality, thus emphasizing the importance of making measurements of protein charge.

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What this paper is about

Abstract The effect of anionic and cationic binding on the surface charge of soy proteins was measured by electrokinetic analysis. All of the ions investigated suppressed the surface charge of the protein; however, certain multivalent ions such as Al (III), Fe (III), hexametaphosphate and tripolyphosphate also altered the isoelectric point of the protein. The results indicated the unpredictability of ionic effects on protein functionality, thus emphasizing the importance of making measurements of protein charge.

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Available abstract

Abstract The effect of anionic and cationic binding on the surface charge of soy proteins was measured by electrokinetic analysis. All of the ions investigated suppressed the surface charge of the protein; however, certain multivalent ions such as Al (III), Fe (III), hexametaphosphate and tripolyphosphate also altered the isoelectric point of the protein. The results indicated the unpredictability of ionic effects on protein functionality, thus emphasizing the importance of making measurements of protein charge.

Key concepts: Isoelectric point, Sodium hexametaphosphate, Electrokinetic phenomena, Surface charge, Chemistry, Soy protein, Ionic bonding, Cationic polymerization

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