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Kinetic behaviour of penicillin acylase stabilized by poly (ethyleneimine)

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Abstract

The paper presents the kinetic evaluations of poly(ethyleneimine)-penicillin acylase preparations. The comparative studies show that the investigated system is much better than the native enzyme, and slightly worse than commercially available Boenringer preparation. Additionally, the high stability of PEI-enzyme system, very easy way of its preparation, high flexibility, and possibility to set the needed enzyme concentration are particularly favourable for use of the membrane bioreactor with PEI-enzyme system immobilized in its volume. Some advantages of the use of such bioreactor are also discussed.

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Abbreviations

C E IU/m3 :

activity concentration

C S mol/m3 :

substrate concentration

C P , CQ mol/m3 :

products concentration

K A mol/m3 :

constant which defines the affinity of a substrate to enzyme

K iS mol/m3 :

substrate inhibitory constant

K iP mol/m3 :

PhAA inhibitory constant

K iQ mol/m3 :

6-APA inhibitory constant

k 3 , mol/IU min:

constant rate of dissociation of the active complex

\(r = - \frac{{dC_S }}{{dt}}\) mol/m3 min:

rate of reaction

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Authors and Affiliations

  1. Institute of Chemical Engineering, Technical University of Wrocław, ul. Norwida 4/6, PL 50-373, Wrocław, Poland

    J. Bryjak & A. Noworyta

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  1. J. Bryjak
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  2. A. Noworyta
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This work was supported by Government Committee of Science: Grant KBN # 3 0321 92 01

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Bryjak, J., Noworyta, A. Kinetic behaviour of penicillin acylase stabilized by poly (ethyleneimine). Bioprocess Engineering 13, 183–187 (1995). https://doi.org/10.1007/BF00367252

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