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Reactivation of thermally inactivated enzymes by free and immobilized chaperonin GroEL/ES

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Abstract

Thermally inactivated bovine deoxyribonuclease I (DNase I) and yeast enolase were reactivated by GroEL/ES from Escherichia coli. In both cases, GroEL/ES was found to have the ability to reactivate inactivated enzymes in an ATP-dependent manner. GroEL/ES can interact with the enzymes that were denatured at high temperature and convert them to the active conformations. To test the applicability of GroEL/ES to the reactivation processes of thermally inactivated enzymes, GroEL/ES was immobilized using formyl-Cellulofine (GroEL/ES-Cellulofine) and its performance was studied. GroEL/ES-Cellulofine retained a sufficiently high ability to reactivate enzymes. Moreover, GroEL/ES-Cellulofine could be used repeatedly, indicating high durability. These results indicate that immobilized chaperonin is effective for reactivation of enzymes that are thermally inactivated in various bioprocesses.

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Authors and Affiliations

  1. Department of Chemical Science and Engineering, Faculty of Engineering, Kobe University, 1-1 Rokkodaicho, Nada, Kobe 657, Japan Fax: +81 78 803 1171, , , , , , JP

    T. Teshima & A. Kondo

  2. Division of Bioscience, The Graduate School of Science and Technology, Kobe University, 1-1 Rokkodaicho, Nada, Kobe 657, Japan, , , , , , JP

    H. Fukuda

Authors
  1. T. Teshima
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  2. A. Kondo
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  3. H. Fukuda
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Received: 16 December 1996 / Received last revision: 21 February 1997 / Accepted: 28 February 1997

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Teshima, T., Kondo, A. & Fukuda, H. Reactivation of thermally inactivated enzymes by free and immobilized chaperonin GroEL/ES. Appl Microbiol Biotechnol 48, 41–46 (1997). https://doi.org/10.1007/s002530051012

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  • DOI: https://doi.org/10.1007/s002530051012

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