Immobilization of lignin peroxidase on nanoporous gold: Enzymatic properties and in situ release of H2O2 by co-immobilized glucose oxidase |
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| Authors: | Huajun Qiu Ying Li Guanglei Ji Guiping Zhou Xirong Huang Yinbo Qu Peiji Gao |
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| Institution: | 1. Key Laboratory of Colloid and Interface Chemistry of the Ministry of Education of China, Shandong University, No. 27 Shanda Nalu, Jinan 250100, PR China;2. State Key Laboratory of Microbial Technology of China, Shandong University, Jinan 250100, PR China |
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| Abstract: | 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 °C higher than that of free LiP. After 2 h 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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| Keywords: | Lignin peroxidase Nanoporous gold Glucose oxidase Co-immobilization Controlled release |
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