Laccase Catalyzed Enamination, Oxidative Coupling, And Immobilized Laccase

laccase, a blue multicopper oxidase, has recently received considerable attentionbecause of its use in oxidizing phenolic and aromatic amine compoundswithconcomitant reduction of oxygen to water. The use of industrial catalyst led toenvironmental pollution. As an important kind of oxidases, without doubt that itsbiological role as a catalyst is important, so its basic research has great significanceand great business value.A new method for the enamination of1,3-dicarbonyl compounds catalyzed bylaccase in water is described for the first time. Besides providing a green and efficientmethod for the synthesis of enaminones, this study extends the applicability of laccasein organic synthesis. Although laccase has advantages such as mild reactiontemperature and pH, but also has disadvantages such as instability as a free enzymeand poorly reuse. These disadvantages make the reaction cost increase. It iswell-known that the immobilization of enzymes on insoluble supports provides aneffective way to perform enzyme reuse and to improve its stability.Trametes villosa Laccase (TVL) was immobilized through physical adsorptionon SBA-15mesoporous silica and the immobilized TVL was used in the oxidativecoupling of trans-resveratrol. The effects of reaction conditions, such as buffer type,pH, temperature and substrate concentration were investigated. In this paper,functionalized ionic liquid modified mesoporous silica SBA-15were synthesized andapplied to immobilize laccase.It was shown that the introduction of functionalized ionic liquid(FIL) influencedthe catalytic behavior of laccase significantly by changing the structure and surfaceproperties of the carrier SBA-15. The secondary structure of Trametes villosa Laccase(TVL) has been studied by FT-IR(Fourier-transform infrared) spectroscopy indifferent solvent and diifferent pH.