Preparation of optically pure tert-leucine by penicillin G acylase-catalyzed resolution.
Penicillin G acylase, from Kluyvera citrophila, was used in kinetic resolution of DL-tert-leucine. N-phenylacetylated-DL-tert-leucine, chemically synthesized from DL-tert-leucine, was enantioselctively hydrolyzed by penicillin G acylase to obtain L-tert-leucine, D-tert-leucine was prepared by acid-catalyzed hydrolysis of the remaining substrate. The total yields of D-tert-leucine and L-tert-leucine are 80.6% and 83.1%, respectively. The enantiomeric excess of the two products, D-tert-leucine and L-tert-leucine, are 98.5% and 99%. This is a practical way for the preparation of D-tert-leucine and L-tert-leucine.
Liu
Shu-Lai
SL
State Key Laboratory of Bioreactor Engineering, New World Institute of Biotechnology, East China University of Science and Technology, Shanghai, P. R. China.
Song
Qing-Xun
QX
Wei
Dong-Zhi
DZ
Zhang
Ye-Wang
YW
Wang
Xue-Dong
XD
D002384:Catalysis; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis; D044086:Kluyvera / Q000201:enzymology; D007930:Leucine / Q000031:analogs & derivatives* / Q000138:chemical synthesis* / Q000737:chemistry; D015394:Molecular Structure; D009904:Optical Rotation; D010399:Penicillin Amidase / Q000378:metabolism*; D010400:Penicillin G / Q000378:metabolism
D010399:Penicillin Amidase; D007930:Leucine; D010400:Penicillin G