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Role of noncovalent forces in micellization using legumin from Vicia faba as a study system
- Ismond, M.A.H., Georgiou, C., Arntfield, S.D., Murray, E.D.
- Journal of food science 1990 v.55 no.6 pp. 1638-1642
- Vicia faba, legumin, thermal properties, hydrophobicity, pH, electrostatic interactions, denaturation
- The seed storage protein, legumin, from Vicia faba interacted to form micelles and elaborate protein networks under varying conditions. Several molecular parameters correlated with observed micelle interaction parameters; these included thermal properties as indicators of protein stability and surface hydrophobicity as an assessment for potential hydrophobic interactions. The optimal pH for micelle formation ranged from 5.5 to 6.5, values at which electrostatic repulsions were minimal and surface hydrophobicites were adequate to allow hydrophobic interactions. The micelle response was affected by anions both in terms of concentration and type of anion. Finally, gradual denaturation of legumin with increasing urea concentrations had a negative impact on the micelle response.