Immobilization of lignin peroxidase on nanoporous gold: enzymatic properties and in situ release of H2O2 by co-immobilized glucose oxidase.
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.
Key Laboratory of Colloid and Interface Chemistry of the Ministry of Education of China, Shandong University, Jinan, PR China.
Huajun
H
Qiu
Ying
Y
Li
Guanglei
G
Ji
Guiping
G
Zhou
Xirong
X
Huang
Yinbo
Y
Qu
Peiji
P
Gao
D004396:Coloring Agents / Q000378:metabolism; D004795:Enzyme Stability; D004800:Enzymes, Immobilized / Q000378:metabolism*; D005949:Glucose Oxidase / Q000378:metabolism*; D006046:Gold / Q000378:metabolism*; D006861:Hydrogen Peroxide / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D053768:Metal Nanoparticles / Q000737:chemistry* / Q000648:ultrastructure; D010544:Peroxidases / Q000378:metabolism*; D016062:Porosity; D012996:Solutions; D013696:Temperature; D013997:Time Factors
D004396:Coloring Agents; D004800:Enzymes, Immobilized; D012996:Solutions; D006046:Gold; D006861:Hydrogen Peroxide; D005949:Glucose Oxidase; D010544:Peroxidases; C042858:lignin peroxidase