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Aggregation Behavior of Bovine kappa- and beta-Casein Studied with Small Angle Neutron Scattering, Light Scattering, and Cryogenic Transmission Electron Microscopy

Ossowski, Sofie; Jackson, Andrew; Obiols-Rabasa, Marc LU ; Holt, Carl; Lenton, Samuel; Porca, Lionel; Paulsson, Marie LU and Nylander, Tommy LU (2012) In Langmuir 28(38). p.13577-13589
Abstract
In the native bovine casein micelle the calcium sensitive caseins (alpha(S1)-, alpha(S2)- and beta-casein) sequester amorphous calcium phosphate in nanometer-sized clusters, whereas the calcium-insensitive K-casein limits the growth of the micelle. In this paper, we further investigate the self-association of kappa- and beta-casein, which are two of the key proteins that control the substructure of the milk casein micelle, using neutron and light scattering techniques and cryogenic transmission electron microscopy. Results demonstrate that K-casein can, apart from the known self-assembly, form amyloid-like fibrils already at temperatures of 25 degrees C when subject to agitation. This extended aggregation behavior of kappa-casein is... (More)
In the native bovine casein micelle the calcium sensitive caseins (alpha(S1)-, alpha(S2)- and beta-casein) sequester amorphous calcium phosphate in nanometer-sized clusters, whereas the calcium-insensitive K-casein limits the growth of the micelle. In this paper, we further investigate the self-association of kappa- and beta-casein, which are two of the key proteins that control the substructure of the milk casein micelle, using neutron and light scattering techniques and cryogenic transmission electron microscopy. Results demonstrate that K-casein can, apart from the known self-assembly, form amyloid-like fibrils already at temperatures of 25 degrees C when subject to agitation. This extended aggregation behavior of kappa-casein is inhibited by beta-casein, as reported by others. These findings have implications for the structure and stability of casein micelles. The neutron scattering data was used to gain information on the self-assembly structure of kappa-casein. beta-Casein shows similar self-association behavior as kappa-casein, but unlike kappa-casein, the self-association exhibits temperature dependence within the studied temperatures (6 and 25 degrees C). Here, we will discuss our extended study of the known self-assembly of casein in the context of the fibrillation of kappa-casein. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Langmuir
volume
28
issue
38
pages
13577 - 13589
publisher
The American Chemical Society
external identifiers
  • wos:000309040800006
  • scopus:84866641501
ISSN
0743-7463
DOI
10.1021/la302416p
language
English
LU publication?
yes
id
b478c224-fe76-49d6-9f0f-76bc05fe5569 (old id 3190112)
date added to LUP
2012-12-04 08:27:03
date last changed
2017-08-06 03:27:59
@article{b478c224-fe76-49d6-9f0f-76bc05fe5569,
  abstract     = {In the native bovine casein micelle the calcium sensitive caseins (alpha(S1)-, alpha(S2)- and beta-casein) sequester amorphous calcium phosphate in nanometer-sized clusters, whereas the calcium-insensitive K-casein limits the growth of the micelle. In this paper, we further investigate the self-association of kappa- and beta-casein, which are two of the key proteins that control the substructure of the milk casein micelle, using neutron and light scattering techniques and cryogenic transmission electron microscopy. Results demonstrate that K-casein can, apart from the known self-assembly, form amyloid-like fibrils already at temperatures of 25 degrees C when subject to agitation. This extended aggregation behavior of kappa-casein is inhibited by beta-casein, as reported by others. These findings have implications for the structure and stability of casein micelles. The neutron scattering data was used to gain information on the self-assembly structure of kappa-casein. beta-Casein shows similar self-association behavior as kappa-casein, but unlike kappa-casein, the self-association exhibits temperature dependence within the studied temperatures (6 and 25 degrees C). Here, we will discuss our extended study of the known self-assembly of casein in the context of the fibrillation of kappa-casein.},
  author       = {Ossowski, Sofie and Jackson, Andrew and Obiols-Rabasa, Marc and Holt, Carl and Lenton, Samuel and Porca, Lionel and Paulsson, Marie and Nylander, Tommy},
  issn         = {0743-7463},
  language     = {eng},
  number       = {38},
  pages        = {13577--13589},
  publisher    = {The American Chemical Society},
  series       = {Langmuir},
  title        = {Aggregation Behavior of Bovine kappa- and beta-Casein Studied with Small Angle Neutron Scattering, Light Scattering, and Cryogenic Transmission Electron Microscopy},
  url          = {http://dx.doi.org/10.1021/la302416p},
  volume       = {28},
  year         = {2012},
}