Abstract
The immobilization of enzymes and other proteins into ordered thin materials has attracted considerable attention over the past few years. This research has demonstrated that biomolecules immobilized in different [Langmuir-Blodgett (LB)/Langmuir-Schaefer (LS)] matrixes retain their functional characteristics to a large extent. These new materials are of interest for applications as biosensors and biocatalysts. We review the growing field of oxidases immobilized onto ordered Langmiur-Blodgett and Langmuir-Schaefer films. Strategies for the preparation of solid supports and the essential properties of the resulting materials with respect to the envisaged applications are presented. Basic effects of the nature of the adsorption and various aspects of the application of these materials as biosensors, biocatalysts are discussed. Outlook of potential applications and further challenges are also provided.
Highlights
Biosensors generally offer simplified reagentless analyses for a range of biomedical and industrial applications and for this reason this area has continued to develop into an ever-expanding and multidisciplinary field during the last years
The effect of equimolar addition of 1 into matrix of linoleic acid and octadecyltrimetyl-ammonium bromide is depicted in Figure 7; an enzyme activity increased more than two times in case of laccase and it retained ca. 70% of its initial activity for as long as 4 months [11]
In order to visualize the deposition of phenolooxidase thin films and to analyze the surface density of prepared protein films, atomic force microscopy (AFM) was employed
Summary
Biosensors generally offer simplified reagentless analyses for a range of biomedical and industrial applications and for this reason this area has continued to develop into an ever-expanding and multidisciplinary field during the last years. Fabricating ordered films involves formation of stable monolayers at the air-liquid interface to be subsequently transferred onto a solid support, which requires a detailed investigation on the mechanisms through which different materials interact at the interface. This is especially important when biomolecules are to be immobilized in LB films, whose biological activity strongly depend on the molecular arrangements [2]. By positioning the substrate horizontally, there is no requirement for the monolayer material to reorganize, as a large area of film is deposited instantly when the horizontal substrate touches the monolayer. Immobilization methods for tyrosinase such as physical adsorption, covalent cross-linking, incorporation within carbon paste, immobilization in polymer films, entrapment in cyro-hydrogel and some sol–gel matrices have been reported in the literature [10]
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