Y. Chikusa, Y. Hirayama, M. Ikunaka
Apr 9, 2003
Citations
0
Influential Citations
28
Citations
Journal
Organic Process Research & Development
Abstract
Chiral, racemic esters, ethyl (±)-tetrahydrofuran-2-carboxylate 4c, methyl (±)-α-phenylpropionate 9b, methyl (±)-5,5-dimethyl-1,3-thiazolidine-4-carboxylate 12a, 2-methoxyethyl (±)-1-(4-tert-butylphenyl)-2-oxopyrrolidine-4-carboxylate 15a, (±)-1-benzyloxy-3-chloropropan-2-yl hydrogen succinate 18c, and (±)-3-butyryloxyquinuclidinium butyrate [(±)-20b·n-PrCO2H], are resolved kinetically by enantioselective hydrolysis catalyzed by an Aspergillus melleus protease [E = 60; 93.9% ee and 35% yield for (R)-tetrahydrofuran-2-carboxylic acid 4a], a Klebsiella oxytoca hydrolase [E > 200; 99.5% ee and 36% yield for (S)-α-phenylpropionic acid 9a], a K. oxytoca hydrolase [E = 145; 97.7% ee and 34% yield for (R)-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid 12b], a Bacillus brevis protease [E = 77; 99% ee and 45% yield for (S)-15a], a Serratia marcescence esterase [E = 49; 99% ee and 43% yield for (S)-18c], and an A. melleus protease [E = 96; 96% ee and 42% yield for (R)-20b], respectively. Each enzymatic process is ...