Enantioselective Hydrolysis of Pentyl Ether 3-Aminobutyric Acid in the Presence of Enzyme Drugs
We investigated the possibility of obtaining enantiomerically pure 3-aminobutyric acid by enantioselective hydrolysis of racemic pentyl ether of 3-aminobutyric acid in the presence of enzyme preparations <i>Candida Antarctica </i>(CAL-B) ( Novozym 435) and Chymotrypsin. Enantioselective hydrolysis of the racemic pentyl ester of 3-aminobutyric acid in the presence of Novozym 435 leads to the formation of 3 R -(-)-3-aminobutyric acid with a yield of 88% of theoretical and optical purity of 86% <i>ee</i>. The yield of residual pentyl ester of 3<i>S</i>-(+)-3-aminobutyric acid was 28% (of theory) and an optical purity of 56% <i>ee</i>. As a result of the partial hydrolysis of racemic pentyl ether of 3-aminobutyric acid in the presence of chymotrypsin 3<i>S</i>-(+)-3-aminobutyric acid is formed with yields of 68% of theoretical and optical purity of 79% <i>ee</i>. The residual pentyl 3<i>R</i>-(-)-3-aminobutyrate was obtained in yields of 60% (of theory) and optical purity of 45% <i>ee</i>.