Resolution of racemic phenylalanine.
نویسنده
چکیده
Phenylalanine has previously been resolved by fractional crystallization of the brucine salt of formyl-nn-phenylalanine (1) or of the cinchonine salt of benzoyl-nn-phenylalanine (2). Enzymatic methods have also been used for the resolution. According to the method of Gilbert, Price, and Greenstein (3), racemic phenylalanine is resolved by subjecting its Nchloroacetylated derivative to asymmetric hydrolysis by a carboxypeptidase present in beef pancreas. A preparation of the enantiomorphs of DL-phenylalanine has also been reported by making use of the difference in rates of synthesis by papain of the anilides of acetyl-nL-phenylalanylglycine (4). In this paper, a simple method is described, which is based upon the asymmetric hydrolysis of the isopropyl ester of DL-phenylalanine by an enzyme preparation derived from pancreas. Complete digestion of the ester yields free L-phenylalanine and the isopropyl ester of n-phenylalanine. The latter is easily separated by virtue of its solubility in ether and alcohol. The ethyl ester of DL-phenylalanine is hydrolyzed in the same manner. However, the isopropyl ester is not hydrolyzed appreciably by water at room temperature and is therefore more suitable for the purpose. Resolution of amino acids by asymmetric hydrolysis of their esters has previously been used to obtain the isomers of leucine (5), methionine (6, 7), and tryptophan (8).
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ورودعنوان ژورنال:
- The Journal of biological chemistry
دوره 186 1 شماره
صفحات -
تاریخ انتشار 1950