User:Andy Maloney/Kinesin & Microtubule Page/Surface passivation/Casein micelle structure a concise review

Disclaimer

These are my notes. Please read the paper before reading my notes.

Paper

Casein micelle structure: a concise review

Notes

• This is a review about the casein micelle.
• There are 3 proposed casein micelle structures:
  • Coat-core
    • An aggregate of caseins with the chell having a different composition
  • Subunit
    • Made up of roughly unifom subunits or micelles
  • Internal structure
    • This tries to specify the mode of aggregation of caseins into the micellular structure.
• Normal bovine milk is about 3.5% protein.
  • 80% of this protein is casein.
  • The rest is whey and glycoproteins.
• The function of the proteins in milk is to supply young with amino acids, nutrients and calcium.
• Heat treatment of milk is okay because of the high heat stability of caseins.
• Main components of bovin casein are the α_s1, α_s2, β, κ-caseins.
• Caseins can be modified post translationally.
• kappa casein has only one phosphoseryl residue which is also glycosylated.
• Caseins have lots of propyl residues on them.
• alpha-caseins are the major casein proteins.
  • They conain about 8-10 seryl phosphate groups.
• beta-caseins contain ~5 phosphoserine residues and are more hydrophobic than alpha and kappa caseins.
• Casein is not heat sensitive.
  • Only at about 120˚C do things change.
• Dry casein is about 94% protein and 6% colloidal calcium phosphate.
• The micelles range in size from 50-500 nm and are on average about 120 nm in diameter.

Take home

This paper again states that casein is heat insensitive. Thus I think I'm justified in believing I can heat a PEM + whole casein mixture in order to get the whole casein into solution.