Abstract:
:The stability of internally cross-linked casein micelles against disruption by urea (which disrupts hydrogen bonds and hydrophobic interactions) and trisodium citrate (which sequesters micellar calcium phosphate) was investigated. Addition of urea (0-6 mol L-1) and/or citrate (0-50 mmol L-1) progressively reduced the turbidity of a suspension of casein micelles cross-linked by transglutaminase and increased particle size (determined by dynamic and static light scattering and small-angle neutron scattering), which was attributed to swelling of the micelles. Furthermore, model calculations, assuming a completely stable casein network, were performed to describe the decreases in turbidity on addition of urea and citrate. Measured and described turbidity values are in agreement, indicating that cross-linking of casein micelles with transglutaminase results in a covalently bound protein network, which is entirely stable to disruption by urea and/or citrate. This may offer potential applications for the use of cross-linked casein micelles as biocompatible protein micro-gel particles.
journal_name
Biomacromoleculesjournal_title
Biomacromoleculesauthors
Huppertz T,Smiddy MA,de Kruif CGdoi
10.1021/bm061070msubject
Has Abstractpub_date
2007-04-01 00:00:00pages
1300-5issue
4eissn
1525-7797issn
1526-4602journal_volume
8pub_type
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