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Covalent immobilization of the multienzyme enniatin synthetase

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Summary

The multienzyme enniatin synthetase was covalently immobilized to N-hydroxysuccinimide activated agarose. The stability of the immobilized enzyme at 25°C was enhanced compared to the soluble enzyme. Immobilization experiments also indicated that the enniatins are synthesized by a single molecule and thus do not require interactions of several enzyme molecules.

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Authors and Affiliations

  1. Pure and Applied Biochemistry, Chemical center, University of Lund, P.O. Box 124, S-220 07, Lund, Sweden

    Nils Siegbahn & Klaus Mosbach

  2. Institute of Biotechnology, ETH, Zürich, Switzerland

    Nils Siegbahn & Klaus Mosbach

  3. Institut fur Biochemie und Molekulare Biologie, Technische Universität Berlin, Franklinstrasse 29, D-1000, Berlin 10

    Karola Grodzki, Rainer Zocher, Norbert Madry & Horst Kleinkauf

Authors
  1. Nils Siegbahn
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  2. Klaus Mosbach
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  3. Karola Grodzki
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  4. Rainer Zocher
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  5. Norbert Madry
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  6. Horst Kleinkauf
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Siegbahn, N., Mosbach, K., Grodzki, K. et al. Covalent immobilization of the multienzyme enniatin synthetase. Biotechnol Lett 7, 297–302 (1985). https://doi.org/10.1007/BF01030274

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  • DOI: https://doi.org/10.1007/BF01030274

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