화학공학소재연구정보센터
Bioresource Technology, Vol.100, No.17, 3837-3842, 2009
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 UP aqueous solution, UP was successfully immobilized on NPG. The optimal temperature of the immobilized UP was ca. 40, 10 degrees C higher than that of free UP. After 2 h incubation at 45 degrees C, 55% of the initial activity of the immobilized UP was still retained while the free UP was completely deactivated. In addition, a high and sustainable UP 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. (C) 2009 Elsevier Ltd. All rights reserved.