Immobilization of lignin peroxidase on nanoporous gold: enzymatic properties and in situ release of H2O2 by co-immobilized glucose oxidase

Bioresour Technol. 2009 Sep;100(17):3837-42. doi: 10.1016/j.biortech.2009.03.016. Epub 2009 Apr 5.


Immobilization of enzymes on porous inorganic materials is very important for biocatalysis and biotransformation. In this paper, nanoporous gold (NPG) was used as a support for lignin peroxidase (LiP) immobilization. NPG with a pore size of 40-50 nm was prepared by dealloying Au/Ag alloy (50:50 wt%) for 17 h. By incubation with LiP aqueous solution, LiP was successfully immobilized on NPG. The optimal temperature of the immobilized LiP was ca. 40, 10 degrees C higher than that of free LiP. After 2h incubation at 45 degrees C, 55% of the initial activity of the immobilized LiP was still retained while the free LiP was completely deactivated. In addition, a high and sustainable LiP activity was achieved via in situ release of H(2)O(2) by a co-immobilized glucose oxidase. The present co-immobilization system was demonstrated to be very effective for LiP-mediated dye decolourization.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Coloring Agents / metabolism
  • Enzyme Stability
  • Enzymes, Immobilized / metabolism*
  • Glucose Oxidase / metabolism*
  • Gold / metabolism*
  • Hydrogen Peroxide / metabolism*
  • Hydrogen-Ion Concentration
  • Metal Nanoparticles / chemistry*
  • Metal Nanoparticles / ultrastructure
  • Peroxidases / metabolism*
  • Porosity
  • Solutions
  • Temperature
  • Time Factors


  • Coloring Agents
  • Enzymes, Immobilized
  • Solutions
  • Gold
  • Hydrogen Peroxide
  • Glucose Oxidase
  • Peroxidases
  • lignin peroxidase