Plant protein-polysaccharide interactions in solutions: application of soft particle analysis and light scattering measurements.
The soft particle analysis theory was applied to plant proteins and polysaccharides in solution, to determine the charge density of these polymers and the depth of the layer accessible by counterions according to pH conditions. In addition to the macromolecule shape characterized by light scattering measurements, these properties are also correlated with the optimum coacervation condition, so as to establish the prevalent plant protein-polysaccharide interactions governing the coacervate formation. Globulin was found to be highly charged and spherically shaped. The best coacervation condition was obtained at the pH value, which corresponds to the protein conformation with a dense and compact accessible layer. On the contrary, for the alpha gliadin, bearing a lower charge, a more extended conformation seems to be more favourable. For the plant proteins studied, the coacervation seems to be controlled by the structure of the counter polyanion used: from our model, it turns out that the rod-like structure of arabic gum observed at acidic pH allows the interaction with plant proteins to form coacervates, contrary to the highly charged and spherical structure of alginate.
Ducel
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INSERM unité 646, Ingéniérie de la Vectorisation Particulaire, 10 rue A. Boquel, 49100 Angers, France.
Saulnier
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Richard
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Boury
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D002236:Carbohydrate Conformation; D004586:Electrophoresis; D005916:Globulins / Q000737:chemistry; D008027:Light; D018532:Pisum sativum / Q000737:chemistry*; D010940:Plant Proteins / Q000737:chemistry*; D011134:Polysaccharides / Q000737:chemistry*; D011487:Protein Conformation; D012542:Scattering, Radiation; D012996:Solutions; D012997:Solvents
D005916:Globulins; D010940:Plant Proteins; D011134:Polysaccharides; D012996:Solutions; D012997:Solvents