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Polyacrylamide gel immobilization of porcine liver esterase for the enantioselective production of levofloxacin

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Abstract

Porcine liver esterase was immobilized in polyacrylamide gel for the enantioselective production of levofloxacin from ofloxacin butyl ester. The initial activity of immobilized esterase was found to be significantly affected by the polyacrylamide gel composition. The optimum concentrations of monomer and crosslinker were determined to be 20% and 8.3%, respectively. The activity of immobilized esterase was 55.4% compared to a free enzyme. Enantiomeric excess was maintained at 60%, almost the same level as that of free enzyme. In addition, the immobilized esterase could be used repeatedly up to 10 times without experiencing any severe loss of activity and enantioselectivity.

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Authors and Affiliations

  1. Department of Biological Engineering and Center for Advanced Bioseparation Technology, Inha University, 402-751, Incheon, Korea

    Sang-Yoon Lee, Byung-Hyuk Min & Dong-Il Kim

  2. Boryung Central Research Institute, Boryung Pharmaceutical Co. Ltd., 425-120, Ansan, Kyungki-do, Korea

    Seong-Won Song, Sun-Young Oh, Sang-Min Lim & Sang-Lin Kim

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  1. Sang-Yoon Lee
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  2. Byung-Hyuk Min
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  3. Seong-Won Song
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  4. Sun-Young Oh
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  5. Sang-Min Lim
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  7. Dong-Il Kim
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Correspondence to Dong-Il Kim.

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Lee, SY., Min, BH., Song, SW. et al. Polyacrylamide gel immobilization of porcine liver esterase for the enantioselective production of levofloxacin. Biotechnol. Bioprocess Eng. 6, 179–182 (2001). https://doi.org/10.1007/BF02932547

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  • DOI: https://doi.org/10.1007/BF02932547

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