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Biotechnology and Applied Biochemistry (2003) 38, (107–110) (Printed in Great Britain)

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Lipase-catalysed enantioselective ammonolysis of phenylglycine methyl ester in organic solvent

Wei Du*¹, Minhua Zong†, Yong Guo† and Dehua Liu*

*Department of Chemical Engineering, Tsinghua University, Beijing 100084, People's Republic of China, and †Department of Biotechnology, South China University of Technology, Guangzhou 510641, People's Republic of China

Key words: ammonolysis, enantioselective, kinetic resolution, lipase, phenylglycine amide.

¹To whom correspondence should be addressed (e-mail duwei@tsinghua.edu.cn).

Ammonium, provided by ammonium carbamate as a novel acyl acceptor, was adopted for enzymic enantio-selective ammonolysis of racemic phenylglycine methyl ester in this paper and it has been found that the reaction conditions have profound effects on enzymic activity and enantioselectivity: the optimal concentration of ammonium carbamate was 80 mM; t-butanol was the most suitable reaction medium and the optimum initial water activity was found to be 0.75; relatively high reaction rate and enantioselectivity could be attained within the temperature range of 30–40 °C. Compared with the corresponding hydrolysis and alcoholysis, enzymic ammonolysis expressed rather high enzymic activity and enantioselectivity and 95% of enzymic activity remained after 10 batches of ammonolysis, which demonstrates that lipase-catalysed ammonolysis is a promising method for the preparation of optically pure (R)-phenylglycine and its derivatives.

Received 22 April 2003; accepted 15 May 2003

Published as Immediate Publication 15 May 2003, DOI 10.1042/BA20030068

© 2003 Portland Press Ltd