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Production of L ‐phenylacetylcarbinol ( L ‐PAC) from benzaldehyde using partially purified pyruvate decarboxylase (PDC)
Author(s) -
Shin Hyoun S.,
Rogers Peter L.
Publication year - 2000
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/(sici)1097-0290(19960105)49:1<52::aid-bit7>3.0.co;2-s
Subject(s) - pyruvate decarboxylase , benzaldehyde , chemistry , biochemistry , carboxy lyases , chromatography , enzyme , catalysis , alcohol dehydrogenase
Biotransformation of benzaldehyde to L ‐phenylacetylcarbinol ( L ‐PAC) as a key intermediate for L ‐ephedrine synthesis has been evaluated using pyruvate decarboxylase (PDC) partially purified from Candida utilis . PDC activity was enhanced by controlled fermentative metabolism and pulse feeding of glucose prior to the enzyme purification. With partially purified PDC, several enzymatic reactions occurred simultaneously and gave rise to by‐products (acetaldehyde and acetoin) as well as L ‐PAC production. Optimal reaction conditions were determined for temperature, pH, addition of ethanol, PDC activity, benzaldehyde, and pyruvate:benzaldehyde ratio to maximize L ‐PAC, and minimize by‐products. The highest L ‐PAC concentration of 28.6 g/L (190.6 m M ) was achieved at 7 U/mL PDC activity and 200 m M benzaldehyde with 2.0 molar ratio of pyruvate to benzaldehyde in 40 m M potassium phosphate buffer (pH 7.0) containing 2.0 M ethanol at 4°C. © 1996 John Wiley & Sons, Inc.