Kinetic resolution of amino acid esters catalyzed by lipases.
Racemic amino acids were resolved by lipase via hydrolysis of their esters. Lipases (Pseudomonas lipase from Amano PS, Rhizopus lipase from Serva, and porcine pancrease lipase from Sigma) could selectively hydrolyze the L-amino acid esters in aqueous solution with high reactivities and selectivities. The effect of the structural changes in the ester moiety on the stereoselectivity of the lipases was also investigated using D,L-homophenylalanine as a model. Procedures were developed for the resolution of natural and unnatural amino acids.
Union Chemical Laboratories, Industrial Technology Research Institute, Hsinchu, Taiwan, Republic of China.
J Y
JY
Houng
M L
ML
Wu
S T
ST
Chen
D000596:Amino Acids / Q000737:chemistry / Q000302:isolation & purification*; D000613:Aminobutyrates / Q000737:chemistry; D002384:Catalysis; D002851:Chromatography, High Pressure Liquid; D004952:Esters / Q000737:chemistry; D006868:Hydrolysis; D007700:Kinetics; D008049:Lipase / Q000378:metabolism*; D013237:Stereoisomerism
D000596:Amino Acids; D000613:Aminobutyrates; D004952:Esters; C014328:2-amino-4-phenylbutyric acid; D008049:Lipase