Adsorption of beta-casein to hydrophilic silica surfaces. Effect of pH and electrolyte
Svensson, Olof LU ; Kurut Sabanoglu, Anil LU and Skepö, Marie LU
(2014)
In Food Hydrocolloids
36.
p.332-338
- Abstract
- Adsorption of beta-casein to hydrophilic silica surfaces has been studied as an effect of pH and electrolyte, in the latter concentration, valency, and specificity (calcium or magnesium) have been considered. The used protein concentration has been an order of magnitude below the critical aggregation concentration, which implies that the protein is in monomeric form. By varying the salt concentration, the pH, and the concentration of divalent ions as calcium and magnesium, it is clearly shown that electrostatic interactions are of importance for adsorption of beta-casein to silica surfaces and tunes the adsorbed amount and saturation of the surface. Our results show that there is counterbalance between: (i) electrostatic repulsion between... (More)
- Adsorption of beta-casein to hydrophilic silica surfaces has been studied as an effect of pH and electrolyte, in the latter concentration, valency, and specificity (calcium or magnesium) have been considered. The used protein concentration has been an order of magnitude below the critical aggregation concentration, which implies that the protein is in monomeric form. By varying the salt concentration, the pH, and the concentration of divalent ions as calcium and magnesium, it is clearly shown that electrostatic interactions are of importance for adsorption of beta-casein to silica surfaces and tunes the adsorbed amount and saturation of the surface. Our results show that there is counterbalance between: (i) electrostatic repulsion between the surface and the protein, (ii) electrostatic attraction between positively charged amino acids in the protein and the surface, and (iii) electrostatic repulsion and excluded volumes between adsorbed proteins at the surface, and that the positively charged amino acids serve as anchoring points. (C) 2013 Elsevier Ltd. All rights reserved. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/4272998
- author
- Svensson, Olof
LU
; Kurut Sabanoglu, Anil
LU
and Skepö, Marie
LU
- organization
- publishing date
- 2014
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- Milk protein, Casein, Surfaces, Hydrophilic silica, Adsorption
- in
- Food Hydrocolloids
- volume
- 36
- pages
- 332 - 338
- publisher
- Elsevier
- external identifiers
-
- wos:000327540500040
- scopus:84887573465
- ISSN
- 0268-005X
- DOI
- 10.1016/j.foodhyd.2013.09.006
- language
- English
- LU publication?
- yes
- additional info
- The information about affiliations in this record was updated in December 2015. The record was previously connected to the following departments: Theoretical Chemistry (S) (011001039)
- id
- 25b73734-34d5-46c2-9626-3d6a3ca76690 (old id 4272998)
- date added to LUP
- 2016-04-01 10:47:33
- date last changed
- 2025-04-04 15:01:28
@article{25b73734-34d5-46c2-9626-3d6a3ca76690,
abstract = {{Adsorption of beta-casein to hydrophilic silica surfaces has been studied as an effect of pH and electrolyte, in the latter concentration, valency, and specificity (calcium or magnesium) have been considered. The used protein concentration has been an order of magnitude below the critical aggregation concentration, which implies that the protein is in monomeric form. By varying the salt concentration, the pH, and the concentration of divalent ions as calcium and magnesium, it is clearly shown that electrostatic interactions are of importance for adsorption of beta-casein to silica surfaces and tunes the adsorbed amount and saturation of the surface. Our results show that there is counterbalance between: (i) electrostatic repulsion between the surface and the protein, (ii) electrostatic attraction between positively charged amino acids in the protein and the surface, and (iii) electrostatic repulsion and excluded volumes between adsorbed proteins at the surface, and that the positively charged amino acids serve as anchoring points. (C) 2013 Elsevier Ltd. All rights reserved.}},
author = {{Svensson, Olof and Kurut Sabanoglu, Anil and Skepö, Marie}},
issn = {{0268-005X}},
keywords = {{Milk protein; Casein; Surfaces; Hydrophilic silica; Adsorption}},
language = {{eng}},
pages = {{332--338}},
publisher = {{Elsevier}},
series = {{Food Hydrocolloids}},
title = {{Adsorption of beta-casein to hydrophilic silica surfaces. Effect of pH and electrolyte}},
url = {{http://dx.doi.org/10.1016/j.foodhyd.2013.09.006}},
doi = {{10.1016/j.foodhyd.2013.09.006}},
volume = {{36}},
year = {{2014}},
}