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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/3190112
- author
- Ossowski, Sofie
; Jackson, Andrew
; Obiols-Rabasa, Marc
LU
; Holt, Carl
; Lenton, Samuel
; Porca, Lionel
; Paulsson, Marie
LU
and Nylander, Tommy
LU
- organization
- publishing date
- 2012
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Langmuir
- volume
- 28
- issue
- 38
- pages
- 13577 - 13589
- publisher
- The American Chemical Society (ACS)
- external identifiers
-
- wos:000309040800006
- scopus:84866641501
- pmid:22924693
- 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
- 2016-04-01 11:12:45
- date last changed
- 2025-10-14 13:29:32
@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 (ACS)}},
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}},
doi = {{10.1021/la302416p}},
volume = {{28}},
year = {{2012}},
}