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Adsorption of proteins at the solution/air interface influenced by added non-ionic surfactants at very low concentrations for both components. 1. Dodecyl dimethyl phospine oxide

Lotfi, M ; Sharif University of Technology

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  1. Type of Document: Article
  2. DOI: 10.1016/j.colsurfa.2014.12.065
  3. Abstract:
  4. The adsorption of proteins at liquid interfaces happens at rather low bulk concentrations due to their rather high surface activity. In contrast typical surfactants start to decrease the surface tension at bulk concentration in the range of mmol/l and reach a minimum value at about two or three orders of magnitude higher concentration. The two proteins studied here, β-lactoglobulin and β-casein, adsorb already remarkably at much lower concentrations, i.e. less than 1. μmol/l. When smallest amounts of a non-ionic surfactant are added to low concentrated protein solutions, changes in the surface tension are observed which cannot be explained by the existing theoretical models. An agreement with the experimental data can be achieved only when an increased surface activity of the protein due to the interaction with the surfactants is assumed
  5. Keywords:
  6. Addition of non-ionic surfactants ; Adsorption of whey proteins BLG and BCS ; Bubble profile analysis tensiometry ; Capillary pressure tensiometry ; Dynamic surface tensions ; Adsorption ; Surface active agents ; Surface tension ; Adsorption of proteins ; Bulk concentration ; Profile analysis tensiometry ; Surface activities ; Three orders of magnitude ; Whey proteins ; Proteins ; 5,5 dimethyl 1 pyrroline 1 oxide ; Beta casein ; Beta lactoglobulin ; Dodecyl dimethyl phospine oxide ; Nonionic surfactant ; Oxide ; Unclassified drug ; Concentration (parameters) ; Controlled study ; Diffusion coefficient ; Priority journal ; Protein interaction ; Surface property ; Surface tension ; Theoretical model ; Thickness
  7. Source: Colloids and Surfaces A: Physicochemical and Engineering Aspects ; Volume 475, Issue 1 , June , 2015 , Pages 62-68 ; 09277757 (ISSN)
  8. URL: http://www.sciencedirect.com/science/article/pii/S0927775715000126