Measurement of the yield stress of gellike protein layers on liquid surfaces by means of an attached particle

Citation
Jt. Petkov et al., Measurement of the yield stress of gellike protein layers on liquid surfaces by means of an attached particle, LANGMUIR, 17(15), 2001, pp. 4556-4563
Citations number
30
Categorie Soggetti
Physical Chemistry/Chemical Physics
Journal title
LANGMUIR
ISSN journal
07437463 → ACNP
Volume
17
Issue
15
Year of publication
2001
Pages
4556 - 4563
Database
ISI
SICI code
0743-7463(20010724)17:15<4556:MOTYSO>2.0.ZU;2-Z
Abstract
We propose a new method for determination of the yield stress of adsorbed p rotein layers on an air-water interface. A small spherical particle is atta ched to the surface, and the latter is deformed by pulling up a barrier att ached to it. When the tangential projection of the gravity force exerted on the particle exceeds a certain threshold, then the layer starts to undergo significant elastic deformation. This is registered as a difference betwee n the experimentally measured particle displacement and that calculated by solving the Laplace equation of capillarity for the liquid boundary. After the yield threshold, there is a linear dependence of the strain on the appl ied stress. We propose a modified Bingham model (two springs and a plastic element) to describe this particular rheological behavior. The elastic modu li found by a linear regression analysis of the stress (strain) relationshi p agree well with literature data for globular proteins. The corresponding yield stress turns out to be very sensitive to changes in the protein layer structure (caused either by the presence of surfactant molecules (Tween 20 ) or by differences in the bulk protein concentration). The threshold stres s monotonically increases with rising protein content, which suggests: a po ssible reinforcement of the adsorbed layer. The addition of Tween 20 brings about surface fluidization. Tween 20 can replace part of the adsorbed prot ein molecules and/or attach to them breaking the intermolecular linkages.