Abstract

ABSTRACTAs a key chiral intermediate of Levetiracetam, (S)‐α‐ethyl‐2‐oxo‐1‐pyrrolidine acetic acid can be produced by ester hydrolase‐catalyzed hydrolysis of (R, S)‐α‐ethyl‐2‐oxo‐1‐pyrrolidine acetic acid ethyl ester. In this paper, the characteristics and kinetics of such hydrolysis were investigated using ester hydrolase derived from soil bacterium Tsukamurella tyrosinosolvens E105. Effects of different parameters were systematically investigated to reveal the primary factors that determine the performance of the enantioselective hydrolysis. The optimal reaction conditions were found to be as follows: temperature, 30 °C; pH, 7.0; potassium phosphate buffer, 0.5 mol/L; and 9.2 mmol/L of substrate. Under the optimum conditions, a substrate inhibition kinetic model based on Michaelis–Menten was proposed and verified with experimental data. Moreover, the obtained kinetic constants were Km = 6.73 mmol/L, Vmax = 18.9 × 10−3 mmol/L/min and Ksi = 23.7 mmol/L. This model can be used to predict the ester hydrolase‐catalyzed hydrolysis of (R, S)‐α‐ethyl‐2‐oxo‐1‐pyrrolidine acetic acid ethyl ester and will be advantageous to the industrial application of this process. © 2014 Curtin University of Technology and John Wiley & Sons, Ltd.

Talk to us

Join us for a 30 min session where you can share your feedback and ask us any queries you have

Schedule a call

Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.