Mass-transfer limitations for immobilized enzyme-catalyzed kinetic resolution of racemate in a fixed-bed reactor

Authors

  • Guo-Hua Xiu,

    Corresponding author
    1. Institute of Chemistry, Chinese Academy of Sciences, Beijing 100080, P.R. China
    Current affiliation:
    1. LSRE Laboratory of Separation and Reaction Engineering, Faculty of Engineering, University of Porto, Rua Dr. Roberto Frias s/n, 4200-465 Porto, Portugal. Telephone: 351-22-5081618; fax: 351-22-5081674
    • Institute of Chemistry, Chinese Academy of Sciences, Beijing 100080, P.R. China
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  • Lei Jiang,

    1. Institute of Chemistry, Chinese Academy of Sciences, Beijing 100080, P.R. China
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  • Ping Li

    1. Department of Chemical Engineering, Shenyang Institute of Chemical Technology, Shenyang, P.R. China
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Abstract

A mathematical model has been developed for immobilized enzyme-catalyzed kinetic resolution of racemate in a fixed-bed reactor in which the enzyme-catalyzed reaction (the irreversible uni–uni competitive Michaelis–Menten kinetics is chosen as an example) was coupled with intraparticle diffusion, external mass transfer, and axial dispersion. The effects of mass-transfer limitations, competitive inhibition of substrates, deactivation on the enzyme effective enantioselectivity, and the optical purity and yield of the desired product are examined quantitatively over a wide range of parameters using the orthogonal collocation method. For a first-order reaction, an analytical solution is derived from the mathematical model for slab-, cylindrical-, and spherical-enzyme supports. Based on the analytical solution for the steady-state resolution process, a new concise formulation is presented to predict quantitatively the mass-transfer limitations on enzyme effective enantioselectivity and optical purity and yield of the desired product for a continuous steady-state kinetic resolution process in a fixed-bed reactor. © 2001 John Wiley & Sons, Inc. Biotechnol Bioeng 74: 29–39, 2001.

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