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Efficient chemoenzymatic synthesis of (S)-α-amino-4-fluorobenzeneacetic acid using immobilized penicillin amidase

Publication date:

October 2018

Source:Bioorganic Chemistry, Volume 80

Author(s): Chao-Ping Lin, Xiao-Ling Tang, Ren-Chao Zheng, Yu-Guo Zheng

An efficient chemoenzymatic route was developed for synthesis of (S)-α-amino-4-fluorobenzeneacetic acid, a valuable chiral intermediate of Aprepitant, using immobilized penicillin amidase catalyzed kinetic resolution of racemic N-phenylacetyl-4-fluorophenylglycine. The optimum temperature, pH and agitation rate of the reaction were determined to be 40 °C, 9.5 and 300 rpm, respectively. Kinetic resolution of 80 g L−1 N-phenylacetyl-4-fluorophenylglycine by immobilized amidase 20 g L−1 resulted in 49.9% conversion and >99.9% e.e. within 3 h. The unreacted N-phenylacetyl-4-fluorophenylglycine can be easily racemized and then recycled as substrate. The production of (S)-α-amino-4-fluorobenzeneacetic acid was further amplified in 1 L reaction system, affording excellent conversion (49.9%) and enantioselectivity (99.9%). This chemoenzymatic approach was demonstrated to be promising for industrial production of (S)-α-amino-4-fluorobenzeneacetic acid.
Graphical abstract

Authors:   Author(s): Chao-Ping Lin, Xiao-Ling Tang, Ren-Chao Zheng, Yu-Guo Zheng
Journal:   Bioorganic Chemistry
Year:   2018
Publication date:   25-Jun-2018
Facts, background information, dossiers
  • production
  • temperature
  • agitation
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