User:Andy Maloney/Kinesin & Microtubule Page/Surface passivation/Dairy Chemistry and Biochemistry Chapter 9
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These are my notes. Please read the book before reading my notes.
- Heating milk causes a decrease in soluable calcium phosphate and it precipitates onto casein micelles. This is reversible through coolin.
- On heating, the pH may decrease due to dephosphorylation of casein.
- Caseins are small 20 - 25 kDa.
- They are relatively hydrophobic
- They have little higher structure, i.e. they do not denature.
- They have few disulphide bonds with alphas2 and kappa caseins being the ones that have them.
- They contain no sulphydrol groups.
- All caseins are phosphorylated.
- alphas1,s2 and beta caseins bind calcium strongly due to their phosphorylation.
- Caseins are not susceptible to thermal denaturation.
- Dephosphorylations does occur to about 100% in one hour if the caseins are heated to 140˚C.
I can heat casein to get it to go into solution!