Abstract
We report on the immobilization of glucose oxidase (GOx) on a silica inverse opal matrix mounted in a configuration to allow reactant to flow through it. Our data show a turnover rate enhancement of up to a factor of ca. 10 for GOx immobilized on the inverse opal structure relative to that of the same enzyme immobilized on a planar silica surface. The surface-immobilized GOx exhibits a factor of 2 turnover rate enhancement relative to that of the enzyme in aqueous solution. The observed enhancements result from two factors, one based on the geometric confinement imposed by the inverse opal structure and the other related to the structural stabilization of GOx because of its (covalent) immobilization on silica. The geometrically derived enhancement predicted by a simple model is mediated by the reaction kinetics of GOx with glucose. These data underscore the significant turnover rate enhancements for catalytic reactions achievable through nanoconfinement.
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