Cupin-1.1 Adsorption Layers at the Surface of 8 M Urea Solutions

The adsorption layers of cupin-1.1, one of the two evolutionary conserved β-barrel domains of vicilin─the garden pea storage globulin─at the liquid-gas interface were studied by a few methods of the surface chemistry. The kinetic dependencies of the surface pressure of cupin-1.1 solutions in 8 M urea overlap in a single master curve if the surface pressure is plotted as a function of the normalized time. The analysis of the master curve allows separation of a few adsorption steps including the induction period, the regions of the diffusion-controlled and barrier-controlled adsorption kinetics, and a plateau region of slow adsorption. Another master curve can be constructed from the dependencies of the dynamic surface elasticity on surface pressure. This curve has some similarities with the corresponding results for recently studied cupin-1.1 spread layers on the surface of urea solutions and gliadin adsorption layers. There are also important distinctions with the master curve for adsorption layers of cupin-1.1 in the system without denaturants. This difference can be connected with the formation of larger and more rigid aggregates in pure water than the aggregates in urea solutions.

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Publication Details

Journal
The Journal of Physical Chemistry B
Published
2024-11-20
DOI
https://doi.org/10.1021/acs.jpcb.4c05607
Citations
1
Primary Topic
Proteins in Food Systems
Type
article
Field-Weighted Citation Impact
0.35

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article

Cupin-1.1 Adsorption Layers at the Surface of 8 M Urea Solutions

G. Loglio, N. A. Isakov, Anton A. Nizhnikov, R. Miller et al.
1 citations
The Journal of Physical Chemistry B
Proteins in Food Systems
0.35
article

Cupin-1.1 Adsorption Layers at the Surface of 8 M Urea Solutions

G. Loglio, N. A. Isakov, Anton A. Nizhnikov, R. Miller, Mikhail V. Belousov, Boris A. Noskov, Amiya Kumar Panda
article en
1 citations

Abstract

The adsorption layers of cupin-1.1, one of the two evolutionary conserved β-barrel domains of vicilin─the garden pea storage globulin─at the liquid-gas interface were studied by a few methods of the surface chemistry. The kinetic dependencies of the surface pressure of cupin-1.1 solutions in 8 M urea overlap in a single master curve if the surface pressure is plotted as a function of the normalized time. The analysis of the master curve allows separation of a few adsorption steps including the induction period, the regions of the diffusion-controlled and barrier-controlled adsorption kinetics, and a plateau region of slow adsorption. Another master curve can be constructed from the dependencies of the dynamic surface elasticity on surface pressure. This curve has some similarities with the corresponding results for recently studied cupin-1.1 spread layers on the surface of urea solutions and gliadin adsorption layers. There are also important distinctions with the master curve for adsorption layers of cupin-1.1 in the system without denaturants. This difference can be connected with the formation of larger and more rigid aggregates in pure water than the aggregates in urea solutions.

The Journal of Physical Chemistry BVol. 128(48)
St Petersburg University (RU), Technische Universität Darmstadt (DE), Vidyasagar University (IN), All-Russian Research Institute of Agricultural Microbiology (RU), Institute of Condensed Matter Chemistry and Technologies for Energy (IT)
Russian Science Foundation
Openalex Percentile: Top 34%
Proteins in Food Systems
0.35
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