Interfacial activity and interfacial shear rheology of native ß-lactoglobulin monomers and their heat-induced fibers
- Jung, Jin-Mi Department of Physics and Fribourg Center for Nanomaterials, University of Fribourg, Switzerland
- Zeynel Gunes, Deniz Department of Food Science and Technology, Nestlé Research Center, Lausanne, Switzerland
- Mezzenga, Raffaele ETH Zurich, Food & Soft Materials Science, Institute of Food, Nutrition & Health, Zurich, Switzerland
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08.09.2010
Published in:
- Langmuir. - 2010, vol. 26, no. 19, p. 15366–15375
English
Interfacial properties of native β-lactoglobulin monomers and their heat-induced fibers, of two different lengths, were investigated at pH 2, through surface tension measurements at water−air and water−oil interfaces and interfacial shear rheology at the water−oil interface. The applied heat treatment generates a mixed system of fibers with unconverted monomers and hydrolyzed peptides. The surface tension of this system at the water−air interface decreased more rapidly than the surface tension of native monomers, especially at short times (10⁻³ to 10²s). This behavior was not observed when the unconverted monomers and peptides were removed by dialysis. At the water−oil interface, the adsorption kinetics was much faster than at the water−air interface, with a plateau interfacial pressure value reached after 1 h of adsorption. For all the systems, interfacial shear rheology showed the formation of a highly elastic interface, with solid-like behavior at 1−10³ s time scales. The highest modulus was observed for the long fibers and the lowest for the native monomers. Creep−compliance curves in the linear regime could be reduced to a single master curve, showing similar spectra of relaxation times for all investigated systems. Upon large deformations, the interfaces formed with long fibers showed the most rigid and fragile behavior. This rigidity was even more pronounced in the presence of unconverted monomers.
- Faculty
- Faculté des sciences et de médecine
- Department
- Département de Physique
- Language
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- English
- Classification
- Physics
- License
- License undefined
- Identifiers
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- RERO DOC 21696
- DOI 10.1021/la102721m
- Persistent URL
- https://folia.unifr.ch/unifr/documents/301838
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