User:Andy Maloney/Kinesin & Microtubule Page/Surface passivation/Casein micelle structure a concise review
These are my notes. Please read the paper before reading my notes.
- This is a review about the casein micelle.
- There are 3 proposed casein micelle structures:
- An aggregate of caseins with the chell having a different composition
- 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.
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.