Resolution of racemic 2-chlorophenyl glycine with immobilized penicillin G acylase

Racemic 2-chlorophenyl glycine has been resolved to obtain (S)-α-amino-(2-chlorophenyl)acetic acid with >99% enantiomeric purity via enantioselective hydrolysis of its N-phenylacetyl derivative with penicillin G acylase immobilized on Eupergit C. The resolution can be conveniently performed in water at substrate concentration of 10% in 5 h with an enzyme:substrate ratio of 1:5 (w/w), and the enzyme can be recycled >25 times without any loss of activity. The unwanted (R)-enantiomer can be easily racemized for recycling.

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(2R)-2-(2-Chlorophenyl)-2-[(2-phenylacetyl)amino]ethanoic acidC16H14ClNO3Ee >99%[α]D25=-96 (c 1, CHCl3)Source of chirality: enzymatic resolutionAbsolute configuration: (R)

(2S)-2-Amino-2-(2-chlorophenylacetyl)ethanoic acidC8H8ClNO2Ee >99%[α]D25=89 (c 1, 1 M HCl)Source of chirality: enzymatic resolutionAbsolute configuration: (S)