Abstract
AbstractThe 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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