Toward controlled geometric structure and surface property
heterogeneities of TiO2 for lipase immobilization
Abstract
Immobilized enzymes as biocatalysts are expected to solve issues of
pollution and economic inefficiency in industrial catalysis. In order to
obtain an immobilized enzyme with high activity and stability, the
design of substrate geometric structure and surface properties is
desirable. Here, TiO2 with controlled pore size and surface properties
was designed and synthesized for lipase immobilization, resulting in an
efficient biocatalyst. The activity of TiO2 immobilized lipase is
improved with the increasing pore size of TiO2 from 10 to 100 nm.
Compared to geometric structure impact, regulation of surface properties
plays a greater role on the immobilization of lipase on TiO2. Among
them, the relative activity of ethenyl triethoxy silane (ETS) modified
TiO2 immobilized lipase is as high as 365.85 % over the pristine
lipase. This research provides experimental evidence for studying the
adsorption of enzyme molecules on the supports under the synergistic
effect of geometric structure and surface properties.