Advanced

Simple Models for Adsorption Kinetics and Their Correlation to the Adsorption of b-Lactoglobulin A and B

Wahlgren, M LU and Elofsson, Ulla (1997) In Journal of Colloid and Interface Science 188(1). p.121-129
Abstract (Swedish)
A description of general models for adsorption kinetics is given. Combinations of the models are compared with adsorption data for the self-associating proteins β-lactoglobulin A and B, from Elofssonet al.(U. M. Elofsson, M. A. Paulsson, and T. Arnebrant,Langmuir,submitted). The adsorption onto methylated silica surfaces was measured by these authors by ellipsometry in phosphate buffer (0.01M,pH 7.0) at five concentrations in the range 0.0003–3 mg/ml. Two models, which agree with the experimental data to a reasonable extent, are presented. These models both contain exchange reactions between adsorbed monomers and dimers from solution. Furthermore, they include three classes of adsorbed molecules, dimers, and two types of monomers. The... (More)
A description of general models for adsorption kinetics is given. Combinations of the models are compared with adsorption data for the self-associating proteins β-lactoglobulin A and B, from Elofssonet al.(U. M. Elofsson, M. A. Paulsson, and T. Arnebrant,Langmuir,submitted). The adsorption onto methylated silica surfaces was measured by these authors by ellipsometry in phosphate buffer (0.01M,pH 7.0) at five concentrations in the range 0.0003–3 mg/ml. Two models, which agree with the experimental data to a reasonable extent, are presented. These models both contain exchange reactions between adsorbed monomers and dimers from solution. Furthermore, they include three classes of adsorbed molecules, dimers, and two types of monomers. The monomer types differ in the rate with which they could be displaced by dimers from the solution. The difference between the two models was in the description of how the less easily displaced monomer form was obtained. In one model they were obtained by an exchange reaction between monomers, dependent on the surface coverage of dimers. In the other they were obtained by displacement of adsorbed monomers by dimers which dissociated upon adsorption. The models could be used to describe the adsorption kinetics of both the A and B variants of β-lactoglobulin at five different concentrations. However, the rate constants differed with a factor of 7.9 between the two proteins, which is of the same size as the difference in the monomer-dimer equilibrium constant. Other models tested, which were found not to fit the data, include for example simple surface dimerization and pure competitive adsorption.

Simple Models for Adsorption Kinetics and Their Correlation to the Adsorption of ??-Lactoglobulin A and B. Available from: https://www.researchgate.net/publication/238641657_Simple_Models_for_Adsorption_Kinetics_and_Their_Correlation_to_the_Adsorption_of_-Lactoglobulin_A_and_B [accessed Jun 22, 2017]. (Less)
Please use this url to cite or link to this publication:
author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Journal of Colloid and Interface Science
volume
188
issue
1
pages
9 pages
publisher
Elsevier
external identifiers
  • scopus:0031126441
ISSN
1095-7103
DOI
10.1006/jcis.1996.4715
language
English
LU publication?
yes
id
57645d5b-3198-4c4e-b709-b43469765067
date added to LUP
2016-04-15 19:30:25
date last changed
2017-06-22 14:58:30
@article{57645d5b-3198-4c4e-b709-b43469765067,
  abstract     = {A description of general models for adsorption kinetics is given. Combinations of the models are compared with adsorption data for the self-associating proteins β-lactoglobulin A and B, from Elofssonet al.(U. M. Elofsson, M. A. Paulsson, and T. Arnebrant,Langmuir,submitted). The adsorption onto methylated silica surfaces was measured by these authors by ellipsometry in phosphate buffer (0.01M,pH 7.0) at five concentrations in the range 0.0003–3 mg/ml. Two models, which agree with the experimental data to a reasonable extent, are presented. These models both contain exchange reactions between adsorbed monomers and dimers from solution. Furthermore, they include three classes of adsorbed molecules, dimers, and two types of monomers. The monomer types differ in the rate with which they could be displaced by dimers from the solution. The difference between the two models was in the description of how the less easily displaced monomer form was obtained. In one model they were obtained by an exchange reaction between monomers, dependent on the surface coverage of dimers. In the other they were obtained by displacement of adsorbed monomers by dimers which dissociated upon adsorption. The models could be used to describe the adsorption kinetics of both the A and B variants of β-lactoglobulin at five different concentrations. However, the rate constants differed with a factor of 7.9 between the two proteins, which is of the same size as the difference in the monomer-dimer equilibrium constant. Other models tested, which were found not to fit the data, include for example simple surface dimerization and pure competitive adsorption. <br/><br/>Simple Models for Adsorption Kinetics and Their Correlation to the Adsorption of ??-Lactoglobulin A and B. Available from: https://www.researchgate.net/publication/238641657_Simple_Models_for_Adsorption_Kinetics_and_Their_Correlation_to_the_Adsorption_of_-Lactoglobulin_A_and_B [accessed Jun 22, 2017].},
  author       = {Wahlgren, M and Elofsson, Ulla},
  issn         = {1095-7103},
  language     = {eng},
  number       = {1},
  pages        = {121--129},
  publisher    = {Elsevier},
  series       = {Journal of Colloid and Interface Science},
  title        = {Simple Models for Adsorption Kinetics and Their Correlation to the Adsorption of b-Lactoglobulin A and B},
  url          = {http://dx.doi.org/10.1006/jcis.1996.4715},
  volume       = {188},
  year         = {1997},
}