Biosensing

Many substrates of laccases are either chromophoric, chromogenic, fluorogenic, chemiluminescent, or electroactive. They may be converted to products suitable (either directly or indirectly via coupled chemical or enzymatic reactions) for optic, electric, or other physical measurements. Thus laccase may be applied as biosensor or bioreporter.

Laccase catalysis, coupled with various physical transducers, could be useful for detecting O2 and a wide variety of reducing substances, especially phenols or anilines [8]. One type of such biosensor may monitor electric signal changes from a modified electrode under the electrocatalysis of a laccase. Another type may detect the photometric change resulted from the oxidation of a chromophoric/ chromogenic substrate. Recent studies include the amperometric detection on laccase-modified electrodes of morphine, phenols, and flavonoids for doping detection, waste monitoring, and beer quality control, respectively [113-116, 116a].

Laccase catalysis may also be used to assay other enzymes. In these assays, either the enzyme of interest catalyzes the production of a compound whose subsequent transformation by laccase generates a detectable physical change, or a product from the laccase catalysis (whose production is accompanied by a detectable physical change) is quenched by the activity of the enzyme of interest. The strategy has been applied to assay various hydrolases, transferases, and oxidore-ductases [8].

Laccase covalently conjugated to bio-binding molecules (for example, antibodies, antigens, DNA, RNA, biotin, or streptavidin) may be used as a reporter for immunochemical, histochemical, cytochemical, or nucleic acid detection assays [8]. In these assays, the binding moiety binds to the target, and the laccase's reaction signals the binding event. Recent progress includes a sandwiched immunosensor and a virtually substrate-free insulin sensor [117, 118].

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