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

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Contents

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 αs1, αs2, 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.

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