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

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Journal of the American Oil Chemists’ Society

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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Authors and Affiliations

  1. Kraft Inc. R&D, 801 Waukegan Rd., 60025, Glenview, IL

    W. S. Chen & W. G. Soucie

Authors
  1. W. S. Chen
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  2. W. G. Soucie
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Chen, W.S., Soucie, W.G. The Ionic Modification of the Surface Charge and Isoelectric Point of Soy Protein. J Am Oil Chem Soc 63, 1346–1350 (1986). https://doi.org/10.1007/BF02679599

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  • DOI: https://doi.org/10.1007/BF02679599

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