Enhancing Biocatalysis: The Case of Unfolded Cytochrome c Immobilized on Kaolinite

Authors

  • Dr. Elena Castellini,

    1. Department of Chemical and Geological Sciences, University of Modena and Reggio Emilia, Via Campi 183, 41125 Modena, Italy
    Search for more papers by this author
  • Dr. Carlo Augusto Bortolotti,

    1. Department of Life Sciences, University of Modena and Reggio Emilia, Via Campi 183, 41125 Modena, Italy, Fax: (+39) 059-373-543
    Search for more papers by this author
  • Dr. Giulia Di Rocco,

    1. Department of Life Sciences, University of Modena and Reggio Emilia, Via Campi 183, 41125 Modena, Italy, Fax: (+39) 059-373-543
    Search for more papers by this author
  • Dr. Fabrizio Bernini,

    1. Department of Chemical and Geological Sciences, University of Modena and Reggio Emilia, Via Campi 183, 41125 Modena, Italy
    Search for more papers by this author
  • Dr. Antonio Ranieri

    Corresponding author
    1. Department of Life Sciences, University of Modena and Reggio Emilia, Via Campi 183, 41125 Modena, Italy, Fax: (+39) 059-373-543
    • Department of Life Sciences, University of Modena and Reggio Emilia, Via Campi 183, 41125 Modena, Italy, Fax: (+39) 059-373-543

    Search for more papers by this author

Abstract

original image

Enhanced catalysis! Urea-unfolded wild-type cytochrome c and its variants immobilized on kaolinite show peroxidase activity that is significantly higher than that of the folded wild-type protein. The accessibility of the substrate to the metal center and the influence of strategic amino acidic residues on the surface of the protein are discussed. This approach sheds light on the factors affecting the catalytic activity of a new versatile biocatalytic interface.

Ancillary