Inside Cover: Oriented Immobilization of Enzymes Made Fit for Applied Biocatalysis: Non-Covalent Attachment to Anionic Supports using Zbasic2 Module (ChemCatChem 8/2011)

Authors

  • Johanna Wiesbauer,

    1. Institute of Biotechnology and Biochemical Engineering, Graz University of Technology, Petersgasse 12/I, 8010 Graz (Austria), Fax: (+43) 316-873-8434
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  • Dr. Juan M. Bolivar,

    1. Institute of Biotechnology and Biochemical Engineering, Graz University of Technology, Petersgasse 12/I, 8010 Graz (Austria), Fax: (+43) 316-873-8434
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  • Dr. Mario Mueller,

    1. Institute of Biotechnology and Biochemical Engineering, Graz University of Technology, Petersgasse 12/I, 8010 Graz (Austria), Fax: (+43) 316-873-8434
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  • Margaretha Schiller,

    1. Institute of Biotechnology and Biochemical Engineering, Graz University of Technology, Petersgasse 12/I, 8010 Graz (Austria), Fax: (+43) 316-873-8434
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  • Prof. Dr. Bernd Nidetzky

    Corresponding author
    1. Institute of Biotechnology and Biochemical Engineering, Graz University of Technology, Petersgasse 12/I, 8010 Graz (Austria), Fax: (+43) 316-873-8434
    2. Co-affiliation of B. Nidetzky: Austrian Research Center of Industrial Biotechnology (ACIB) GmbH, Petergasse 14, 8010 Graz (Austria)
    • Institute of Biotechnology and Biochemical Engineering, Graz University of Technology, Petersgasse 12/I, 8010 Graz (Austria), Fax: (+43) 316-873-8434

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Abstract

original image

The inside cover picture shows the structural model of sucrose phosphorylase from Leuconostoc mesenteroides fused to a positively charged Zbasic2 module that is placed next to a carrier surface showing the opposing (negative) charge. In their Communication on p. 1299 ff., B. Nidetzky et al., describe that non-covalent attachment to ionic supports is a very useful approach for a reversible oriented immobilization of a number of enzymes. High protein loading and excellent catalytic effectiveness of the carrier-bound enzymes can be achieved.

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