Document Detail

Aggregation Behaviour of Bovine κ- and β-Casein studied with Small Angle Neutron Scattering, Light Scattering and Cryogenic Transmission Electron Microscopy.
MedLine Citation:
PMID:  22924693     Owner:  NLM     Status:  Publisher    
In the native bovine casein micelle the calcium sensitive caseins (αS1-, αS2- and β-casein) sequester amorphous calcium phosphate in nm-sized clusters whereas the calcium-insensitive κ-casein limits the growth of the micelle. In this paper we further investigate the self-association of κ- and β-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 κ-casein can, apart from the known self-assembly, form amyloid like fibrils already at temperatures of 25°C when subject to agitation. This extended aggregation behaviour of κ-casein is inhibited by β-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 κ-casein. β-Casein shows similar self-association behaviour as κ-casein, but unlike κ-casein the self-association exhibits temperature dependence within the studied temperatures (6°C and 25°C. Here we will discuss our extended study of the known self-assembly of casein in the context of the fibrillation of κ-casein.
Sofie Ossowski; Andrew Jackson; Marc Obiols-Rabasa; Carl Holt; Samuel Lenton; Lionel Porcar; Marie Paulsson; Tommy Nylander
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Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2012-8-27
Journal Detail:
Title:  Langmuir : the ACS journal of surfaces and colloids     Volume:  -     ISSN:  1520-5827     ISO Abbreviation:  Langmuir     Publication Date:  2012 Aug 
Date Detail:
Created Date:  2012-8-28     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  9882736     Medline TA:  Langmuir     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
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