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  β-Lactoglobulin adsorption layers at the water/air surface: 2. Dilational rheology: Effect of pH and ionic strength

Ulaganathan, V., Retzlaff, I., Won, J., Gochev, G., Gunes, D. Z., Gehin-Delval, C., et al. (2017). β-Lactoglobulin adsorption layers at the water/air surface: 2. Dilational rheology: Effect of pH and ionic strength. Colloids and Surfaces A: Physicochemical and Engineering Aspects, 521, 167-176. doi:10.1016/j.colsurfa.2016.08.064.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002C-0819-5 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002D-4BD2-2
Genre: Journal Article

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Ulaganathan, Vamseekrishna1, Author              
Retzlaff, I.1, Author              
Won, Jooyoung1, Author              
Gochev, Georgi1, Author              
Gunes, D. Z., Author
Gehin-Delval, C., Author
Leser, M., Author
Noskov, B. A., Author
Miller, Reinhard1, Author              
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1Reinhard Miller, Biomaterialien, Max Planck Institute of Colloids and Interfaces, Max Planck Society, ou_1863501              

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 Abstract: The dynamic surface pressure Π and the two components E’ (real part) and E” (imaginary part) of the dynamic surface dilational modulus of adsorbed β-lactoglobulin (BLG) layers at the water/air interface were measured by oscillating drop/bubble profile analysis tensiometry with the aim to enlarge information on the surface rheology of solutions of this practically important protein. The effects of the solution pH and ionic strength (represented by the buffer concentration Cbuff) on the kinetic dependences of Π, E’ and E” were monitored for various protein concentrations in the range 5×10−9–2×10−4 M. Combining the E’(t) and E”(t) data with the Π(t) data allowed for obtaining the dependences E’(Π) and E”(Π). The real part E’ was found to increase monotonically with increasing Π, while the E”(Π) data exhibit a maximum in the surface pressure range 14–18 mN/m. The height of the maximum in the E”(Π) dependence was found to increase with increasing protein concentration. Apparently, in these interfacial layers, relaxation processes take place and their relaxation strengths depend on the history of the layer formation, i.e. the rate of adsorption. After the maximum in the E”(Π) dependence the E”-values progressively diminish, which can be assumed to occur due to solidification of the protein gel-like network accompanied by less energy dissipation and high elasticity of the interfacial layer. BLG layers at pH 5 (close to the isoelectric point pI ≈ 5.1) exhibit the highest E’-values and the lowest E”-values measured in this study, which suggest the formation of a strong protein network at these (isoelectric) conditions. Variations of the buffer concentration strongly influence the kinetic dependences of E’ and E” for BLG layers at pH ≠ pI, while at pH → pI no effect was detected. The viscoelastic characteristics of BLG layers adsorbed from buffer-free solutions containing NaCl or CaCl2 were also studied. For the first time, hysteresis in the frequency dependence of the surface dilational modulus of protein layers measured during repeating cycles of oscillations is reported. Such hysteresis is typical for BLG layers adsorbed at any solution conditions used in this study.

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 Dates: 2016-08-302017-05-20
 Publication Status: Published in print
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 Identifiers: DOI: 10.1016/j.colsurfa.2016.08.064
BibTex Citekey: Ulaganathan2016
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Title: Colloids and Surfaces A: Physicochemical and Engineering Aspects
Source Genre: Journal
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Publ. Info: Amsterdam : Elsevier
Pages: - Volume / Issue: 521 Sequence Number: - Start / End Page: 167 - 176 Identifier: ISSN: 0927-7757