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Interactions between gelatin and sodium dodecyl sulphate: binding isotherm and solution properties
Authors:C?Buron  C?Filiatre  F?Membrey  Email author" target="_blank">A?FoissyEmail author  J?F?Argillier
Institution:(1) LCMI, U.F.R. Sciences et Techniques, 16 Route de Gray, 25030 Besançon cedex, France;(2) Institut Français du pétrole, 1–5 Avenue Bois Préau, Rueil-Malmaison, France
Abstract:The interaction between sodium dodecyl sulphate (SDS) and gelatin was studied at pH 4.5 and 6.5 where the gelatin is positively charged (i.e.p. 8). At pH 4.5 a SDS/gelatin concentration range was found where gelatin precipitates. At pH 6.5 the SDS-gelatin complex remains soluble although three SDS concentration domains were distinguished where the SDS-gelatin complex had very different affinities for the solvent. Below C1 the complex was highly surface active but other measurements (viscosity, potentiometry, protons uptake) did not reveal any particular consequence of binding. Between C1 and C2 the molecular size decreased (viscosity lowering) upon charge neutralization and collapse about small SDS aggregates (17 SDS molecules per gelatin molecule). Above C2 a cooperative binding mechanism lead to the formation of SDS aggregates; the complex stretched out and turned strongly hydrophilic (the viscosity increases, low surface activity). At saturation one gelatin molecule bound about 200 SDS molecules. Above the overlap concentration (about 3 wt%) SDS aggregates formed between several gelatin molecules, the viscosity increased continuously with SDS concentration and the binding ratio was lower than in dilute gelatin solutions. A very good correspondence was found between the different analytical data including turbidity, viscosity, surface tension, protons uptake and direct potentiometric SDS binding measurements.
Keywords:Surfactant-gelatin interaction  Surfactant-protein complexation  Sodium dodecyl sulfate  Surface tension  Viscosity
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