On the adsorption properties of surface-chemically pure aqueous solutions of n-alkyl-dimethyl and n-alkyl-diethyl phosphine oxides

Lunkenheimer, Klaus; Haage, K.; Miller, R.

doi:10.1016/0166-6622(87)80221-4

Cited by 65 publications

(60 citation statements)

References 23 publications

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“…The used water was surface chemically pure (γ 0 =72.0 mN/m at 24°C) MilliQ water. The used surfactant was C 12 dimethyl phosphine oxide (C 12 DMPO) synthesised at the MPI [27]. The solutions were prepared in a pH 7 buffer solution using MilliQ water.…”

Section: Methodsmentioning

confidence: 99%

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Drop profile analysis tensiometry with drop bulk exchange to study the sequential and simultaneous adsorption of a mixed β-casein /C12DMPO system

et al. 2008

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The formation of mixed protein/surfactant adsorption layers is studied by the drop profile analysis tensiometry equipped with a special tool for drop volume exchange during experiments. This arrangement allows investigating in the traditional way by simultaneous adsorption from a mixed solution and also by a subsequent adsorption of the protein followed by surfactant. The experiments are performed for β-casein as the protein in the presence of different amounts of the non-ionic surfactant C 12 DMPO. The surface layers formed via the two routes show similar equilibrium surface properties. However, the dynamics of desorption of the protein complexes into the pure buffer solution deviate significantly, which is explained by the different locations of the protein/surfactant interaction. Although in both cases the complex formation is based on hydrophobic interaction, the accessibility of the hydrophobic parts of pre-adsorbed proteins due to unfolding is more favourable by the surfactant than in the solution bulk. Therefore, the amount desorbed from surface layers formed from mixed solutions is significantly less as compared to the displacement of proteins by subsequently injected surfactants interacting at the surface.

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Section: Methodsmentioning

confidence: 99%

“…β-casein is one of the most frequently investigated model proteins [24][25][26] and the non-ionic alkyl dimethyl phosphine oxides represent an excellent model surfactants for fundamental investigations [27]. The formation of mixed surface layers formed by proteins and surfactants was the example studied in [18,22,[28][29][30][31].…”

Section: Introductionmentioning

confidence: 99%

Drop profile analysis tensiometry with drop bulk exchange to study the sequential and simultaneous adsorption of a mixed β-casein /C12DMPO system

et al. 2008

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“…For both surfactants at all concentrations the is corroborated by calculations of the characteristic diffusion dependencies a(n) can be approximated by straight lines. time of C 12 DMPO (24). In the following only the results of This fact can be explained by a relatively restricted interval measurements for solutions with an adsorption time less than of the investigated frequencies.…”

Section: Resultsmentioning

confidence: 90%

“…The function l(log c) is determined by the surface tension and the shape of the corresponding curves is close to the shape of the surface tension isotherms (Figs. from surface tension measurements (24). In contrast, the damping coefficient of capillary waves sponding region of concentrations turns out to be inapis determined mainly by the dynamic surface elasticity proachable for experimental investigation because of the and the dependency a( log c ) turns out to be significantly too slow establishment of the adsorption equilibrium.…”

Section: Resultsmentioning

confidence: 94%

“…The dependence of surface expressions for 1(v) can be obtained with the help of nonequilibrium thermodynamics (2,3). It is noteworthy that tension on concentration is described by a Frumkin equation (24) and the adsorption process is determined by a simple the theory of surface viscoelasticity cannot be constructed by analogy with the corresponding three-dimensional theory. diffusion mechanism (25).…”

Section: Introductionmentioning

confidence: 99%

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