I guess the isoelectric precipitation is favorable one but it can denature the protein.If so,why this method is used?Can you please explain it?
See if this helps:
https://www.apsu.edu/sites/apsu.edu/files/chemistry/SP11_1021_ISOLATION_OF_PROTEINS_FROM_MILK.pdf
in general you can also try precipitating proteins using equal volume of acetone and incubating at 4 deg C for 24hrs and obtain protein as precipitates which can centrifuged and seperated.
The content of casein in milk is determined by two measurements of infrared absorbance in a milk sample by infrared spectrometry before and after a separation of the casein. The casein content is calculated by use of absorbance data recorded during the two absorbance measurements. The new method is considerable faster than the known wet-chemical methods, such as the normal wet chemical reference method for casein determination in milk using a Kjeldahl nitrogen determination of the milk sample, then a coagulation of the milk, and finally a Kjeldahl nitrogen determination of the filtrate. Further the new method provides a more reliable accuracy than the know determination using a single infrared analysis of a milk sample.
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