Enzyme Technology of Peroxidases: Immobilization, Chemical and Genetic Modification



An overview of enzyme technology applied to peroxidases is made. Immobilization on organic, inorganic, and hybrid supports; chemical modification of amino acids and heme group; and genetic modification by site-directed and random mutagenesis are included. Different strategies that were carried out to improve peroxidase performance in terms of stability, selectivity, and catalytic activity are analyzed. Immobilization of peroxidases on inorganic and organic materials enhances the tolerance of peroxidases toward the conditions normally found in many industrial processes, such as the presence of an organic solvent and high temperature. In addition, it is shown that immobilization helps to increase the Total Turnover Number at levels high enough to justify the use of a peroxidase-based biocatalyst in a synthesis process. Chemical modification of peroxidases produces modified enzymes with higher thermostability and wider substrate variability. Finally, through mutagenesis approaches, it is possible to produce modified peroxidases capable of oxidizing nonnatural substrates with high catalytic activity and affinity.


Random Mutagenesis Phthalic Anhydride Mesoporous Silicate Codon Change Free Carboxylic Group 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.



Acknowledgment for support of this work is made to National Council of Science and technology (CONACyT I003-CB2007-01-80986), PROMEP/103.5/09/4194, and ICyTDF PIFUTP08 148.


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Copyright information

© Springer-Verlag Berlin Heidelberg 2010

Authors and Affiliations

  • Adriana Longoria
    • 1
  • Raunel Tinoco
    • 1
  • Eduardo Torres
    • 2
  1. 1.Instituto de BiotecnologíaUNAMCuernavacaMéxico
  2. 2.Centro de QuímicaBenemérita Universidad Autónoma de PueblaPueblaMéxico

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