Immobilization of lignin peroxidase on nanoporous gold: Enzymatic properties and in situ release of H₂O₂ by co-immobilized glucose oxidase
2009
Qiu, Huajun | Li, Ying | Ji, Guanglei | Zhou, Guiping | Huang, Xirong | Qu, Yinbo | Gao, Peiji
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 40-50nm was prepared by dealloying Au/Ag alloy (50:50wt%) for 17h. By incubation with LiP aqueous solution, LiP was successfully immobilized on NPG. The optimal temperature of the immobilized LiP was ca. 40, 10°C higher than that of free LiP. After 2h incubation at 45°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 H₂O₂ by a co-immobilized glucose oxidase. The present co-immobilization system was demonstrated to be very effective for LiP-mediated dye decolourization.
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