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Lysozyme in catanionic surfactant mixtures

Stenstam, Anna LU ; Khan, Ali LU and Wennerström, Håkan LU (2004) In Langmuir 20(18). p.7760-7765
Abstract
We investigate the competition between the associations of oppositely charged protein-surfactant complexes and oppositely charged surfactant complexes. In all systems examined, the most favorable complexation is the one between the two oppositely charged surfactant ions, despite the strong binding known, for example, dodecyl sulfate, DS-, to lysozyme. Thus, the phase behavior of the catanionic system is dominating the features observed also in the presence of protein. The phase behavior of the dilute protein-free dodecyltrimethylammonium chloride-sodium dodecyl sulfate-water system is presented and used as a basis for the discussion on the different solubilization mechanisms. Our results show that the mechanism for resolubilization of a... (More)
We investigate the competition between the associations of oppositely charged protein-surfactant complexes and oppositely charged surfactant complexes. In all systems examined, the most favorable complexation is the one between the two oppositely charged surfactant ions, despite the strong binding known, for example, dodecyl sulfate, DS-, to lysozyme. Thus, the phase behavior of the catanionic system is dominating the features observed also in the presence of protein. The phase behavior of the dilute protein-free dodecyltrimethylammonium chloride-sodium dodecyl sulfate-water system is presented and used as a basis for the discussion on the different solubilization mechanisms. Our results show that the mechanism for resolubilization of a protein-surfactant salt is fundamentally different when it is caused by addition of a second surfactant than when it is accomplished by an excess of the first surfactant. The competition between lysozyme and cationic amphiphiles as hosts for the anionic surfactants was studied experimentally and analyzed quantitatively. Aggregates with C-12 cationic surfactants are clearly preferred by the anionic surfactants, while for C-10 and particularly C-8 a clear excess of cationic surfactant has to be added to completely dissolve the complex salt lysozyme-anionic surfactant. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Langmuir
volume
20
issue
18
pages
7760 - 7765
publisher
The American Chemical Society
external identifiers
  • pmid:15323529
  • wos:000223567900059
  • scopus:4444342321
ISSN
0743-7463
DOI
10.1021/la049508w
language
English
LU publication?
yes
id
1d9a4f0d-571b-4637-b00c-0effba16a7aa (old id 153791)
date added to LUP
2007-07-12 12:01:24
date last changed
2017-02-05 03:36:50
@article{1d9a4f0d-571b-4637-b00c-0effba16a7aa,
  abstract     = {We investigate the competition between the associations of oppositely charged protein-surfactant complexes and oppositely charged surfactant complexes. In all systems examined, the most favorable complexation is the one between the two oppositely charged surfactant ions, despite the strong binding known, for example, dodecyl sulfate, DS-, to lysozyme. Thus, the phase behavior of the catanionic system is dominating the features observed also in the presence of protein. The phase behavior of the dilute protein-free dodecyltrimethylammonium chloride-sodium dodecyl sulfate-water system is presented and used as a basis for the discussion on the different solubilization mechanisms. Our results show that the mechanism for resolubilization of a protein-surfactant salt is fundamentally different when it is caused by addition of a second surfactant than when it is accomplished by an excess of the first surfactant. The competition between lysozyme and cationic amphiphiles as hosts for the anionic surfactants was studied experimentally and analyzed quantitatively. Aggregates with C-12 cationic surfactants are clearly preferred by the anionic surfactants, while for C-10 and particularly C-8 a clear excess of cationic surfactant has to be added to completely dissolve the complex salt lysozyme-anionic surfactant.},
  author       = {Stenstam, Anna and Khan, Ali and Wennerström, Håkan},
  issn         = {0743-7463},
  language     = {eng},
  number       = {18},
  pages        = {7760--7765},
  publisher    = {The American Chemical Society},
  series       = {Langmuir},
  title        = {Lysozyme in catanionic surfactant mixtures},
  url          = {http://dx.doi.org/10.1021/la049508w},
  volume       = {20},
  year         = {2004},
}