During acid hydrolysis of milk proteins to determine amino acids in casein I did not get the peaks of glutamine and asparagine and when I search about the reason I fond that the are converted into glutamic acid and aspartic acid (Asn) .
how can I determine the concentration of glutamine and asparagine ?
At this point you can only report the sum of aspagarine plus aspartic acid or glutamine plus glutamic acid. You need to use another way of hydrolysing in which the amines are not converted to get results on the amines.
thank you Kan for your answer ,what is the best method to hydrolysis protein for determination of amino acids?
glutamine and asparagine can each be liberated from proteins and peptides without deamidation and determined quantitatively by specific assay ...
In most of the cases it is not possible to detect Glutamate and Glutamine, Aspartate and Asparagine at same time. In most of the cases you will get only the peaks of Glutamate and Aspartate. According to many experts during acid hydrolysis with 6M HCl or 4M Methanesulfonic acid, Glutamine and Asparagine will be converted into the Glutamate and Aspartate respectively. At this point you have to give your result as Glutamine + Glutamate and Asparagine + Aspartate.
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