Degradation of MXC by host/guest-type immobilized laccase on magnetic tubular mesoporous silica

Eco-Friendly Composite of Fe3O4-Reduced Graphene Oxide Particles for Efficient Enzyme Immobilization

“…RGO-Fe 3 O 4 -M1 and rGO particles had similar IYs. The IEs observed herein on rGO-Fe 3 O 4 -M1 particles were much higher than those reported previously for the immobilization of Trametes versicolor laccase, where IEs were reported in the ranges of 20.0–91.0%, ,,− and HRP, where IEs were reported to be 55.5 and 77.5% on magnetic composite particles. HRP immobilized on rGO-Fe 3 O 4 -M1 particles retained up to a 7-fold higher IE than that of the chemically different rGO particles .…”

“…To determine optimum incubation time, 1 mg of enzyme was added to the reaction mixture, and immobilization was monitored over a period of 12 h. Furthermore, enzyme loading onto the particle was measured by increasing the enzyme concentration from 50 to 600 mg/g of support in the reaction mixture under optimum incubation conditions. to those of the free enzyme than magnetic particles composites with either silica 18,39,41,42 or chitosan. 40 Enzyme Stability and Reusability.…”

“…Interestingly, these spherical and porous particles fare much better in reusability than tubular magnetic composite particles, where immobilized laccase lost about 35% of residual activity after only 6 cycles. 39 Additionally, immobilized lipase on chemically modified yolk−shell silica spheres lost 39.7% of activity after only the first cycle, 45 and immobilized β-glucuronidase on graphene/γ-Fe 2 O 3 hybrid aerogels lost 59% of activity after 5 cycles of reuse. 46 Similarly, HRP immobilized onto rGO-Fe 3 O 4 -M1, rGO, and Fe 3 O 4 retained 89.8, 71.8, and 11.7% of their initial activities after 10 cycles of reuse for the oxidation of phenol, respectively (Figure S18c).…”

Reactivity of CuIN4 Flattened Complexes: Interplay between Coordination Geometry and Ligand Flexibility

“…In multicopper oxidases, such as laccase, the active center catalyzes the four-electron reduction of O 2 to water. The tricopper active center in laccase has been a role model for multinuclear copper complexes able to conduce the oxygen reduction reaction (ORR) in electrocatalytic systems, mainly motivated by the development of low-temperature fuel cells. , Laccase and related copper-containing enzymes have also been explored for applications of environmental interest, given its ability to perform dehalogenation reactions in polyhalogenated aromatic substrates, considered as severe contaminants in water effluents and soils. − Bio-inspired mono- and polynuclear copper complexes can also react with halogenated substrates, and the reductive dehalogenation has been proposed as the reaction mechanism. − …”

Development and Characterization of Laccase Based Crosslinked Enzyme Aggregates (Cleas)

“…Development of CLEAs is of great interest due to their higher stability against pH and temperature. Crosslinked aggregates of laccase have multiple applications in waste water treatment, decolorization of dyes, in leathery and textile industries and in agricultural waste management system [4][5][6][7]. Keeping all the aforementioned considerations in view, the aim of the proposed research is to produced and characterize the developed enzyme aggregates and comparatively analyze the thermal stability and reusability of free and insolubilized enzyme.…”