Preparation, optimization, and structures of cross-linked enzyme aggregates (CLEAs)

Authors

  • R. Schoevaart,

    1. Biocatalysis and Organic Chemistry, Department of Biotechnology, Delft University of Technology, Julianalaan 136, 2628 BL Delft, The Netherlands; telephone: + 31 15 2782683; fax: + 31 15 2781415
    2. Industrial Fermentative Chemistry, Leiden University, P.O. Box 9502, 2300 RA Leiden, The Netherlands
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  • M.W. Wolbers,

    1. Bioseparation Technology, Department of Biotechnology, Delft University of Technology, Julianalaan 67, 2628 BC Delft, The Netherlands
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  • M. Golubovic,

    1. Bioseparation Technology, Department of Biotechnology, Delft University of Technology, Julianalaan 67, 2628 BC Delft, The Netherlands
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  • M. Ottens,

    1. Bioseparation Technology, Department of Biotechnology, Delft University of Technology, Julianalaan 67, 2628 BC Delft, The Netherlands
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  • A.P.G. Kieboom,

    1. Industrial Fermentative Chemistry, Leiden University, P.O. Box 9502, 2300 RA Leiden, The Netherlands
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  • F. van Rantwijk,

    1. Biocatalysis and Organic Chemistry, Department of Biotechnology, Delft University of Technology, Julianalaan 136, 2628 BL Delft, The Netherlands; telephone: + 31 15 2782683; fax: + 31 15 2781415
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  • L.A.M. van der Wielen,

    1. Bioseparation Technology, Department of Biotechnology, Delft University of Technology, Julianalaan 67, 2628 BC Delft, The Netherlands
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  • R.A. Sheldon

    Corresponding author
    1. Biocatalysis and Organic Chemistry, Department of Biotechnology, Delft University of Technology, Julianalaan 136, 2628 BL Delft, The Netherlands; telephone: + 31 15 2782683; fax: + 31 15 2781415
    • Biocatalysis and Organic Chemistry, Department of Biotechnology, Delft University of Technology, Julianalaan 136, 2628 BL Delft, The Netherlands; telephone: + 31 15 2782683; fax: + 31 15 2781415
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Abstract

The broad applicability of the cross-linking of enzyme aggregates to the effective immobilisation of enzymes is demonstrated and the influence of many parameters on the properties of the resulting CLEAs is determined. The relative simplicity of the operation ideally lends itself to high-throughput methodologies. The aggregation method was improved up to 100% activity yield for any enzyme. For the first time, the physical structures of CLEAs are elucidated. © 2004 Wiley Periodicals, Inc.

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