Immobilization of Aspergillus sp. laccase on hierarchical silica MFI zeolite with embedded macropores

Tocco, Davide; Wisser, Dorothea; Fischer, Marcus; Schwieger, Wilhelm; Salis, Andrea; Hartmann, Martin

doi:10.1016/j.colsurfb.2023.113311

Cited by 6 publications

(7 citation statements)

References 71 publications

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“…These results indicate that kinetic parameters are affected by the nature of the carrier and by the type of immobilization. However, because of the specific conditions of the activity assays (e.g., pH), an accurate comparison of our results with those reported in the literature is often difficult [ 44 ].…”

Section: Resultsmentioning

confidence: 99%

Construction of Immobilized Laccase System Based on ZnO and Degradation of Mesotrione

Yue,

Wang,

Zhang

et al. 2024

Toxics

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Mesotrione (MES) is a new environmental pollutant. Some reports have indicated that microbial enzymes could be utilized for MES degradation. Laccase is a green biocatalyst whose potential use in environmental pollutant detoxification has been considered limited due to its poor stability and reusability. However, these issues may be addressed using enzyme immobilization. In the present study, we sought to optimize conditions for laccase immobilization, to analyze and characterize the characteristics of the immobilized laccase, and to compare its enzymatic properties to those of free laccase. In addition, we studied the ability of laccase to degrade MES, and analyzed the metabolic pathway of MES degradation by immobilized laccase. The results demonstrated that granular zinc oxide material (G-ZnO) was successfully used as the carrier for immobilization. G-ZnO@Lac demonstrated the highest recovery of enzyme activity and exhibited significantly improved stability compared with free laccase. Storage stability was also significantly improved, with the relative enzyme activity of G-ZnO@Lac remaining at about 54% after 28 days of storage (compared with only 12% for free laccase). The optimal conditions for the degradation of MES by G-ZnO@Lac were found to be 10 mg, 6 h, 30 °C, and pH 4; under these conditions, a degradation rate of 73.25% was attained. The findings of this study provide a theoretical reference for the laccase treatment of 4-hy-droxyphenylpyruvate dioxygenase (HPPD)-inhibiting herbicide contamination.

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Section: Resultsmentioning

confidence: 99%

Construction of Immobilized Laccase System Based on ZnO and Degradation of Mesotrione

Yue,

Wang,

Zhang

et al. 2024

Toxics

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“…On the other hand, reports suggest that the immobilization of laccase on non‐magnetic support shows lower activity recovery after 5 cycles compared to m‐CLEAS as they are recovered by centrifugation [8,33,34] . Centrifugal force can cause aggregation of the various forms of immobilized laccase, resulting in decreased activity and accentuating mass transfer limitations.…”

Section: Resultsmentioning

confidence: 99%

“…The protein concentration was directly determined for free enzyme and CLEAS. However, for m‐CLEAS the protein concentration was estimated as the unbound protein in the supernatant ([P] s ) and then subtracted from the total amount of protein initially used in the reaction for the synthesis ([P] 0 ) [8,26] . The samples (100 μL) were mixed with BioRad reagent (900 μL) in a plastic cuvette and after 10 min the absorption was measured at 595 nm using UV‐Vis spectrophotometer.…”

Section: Methodsmentioning

confidence: 99%

“…Immobilizing laccase on insoluble support has become a popular method to improve enzyme stability, reusability, and bioactivity. A variety of carriers including membrane, [4] nanoparticles, [5,6] microspheres, [7] zeolites, [8] and nanofibers [9] have been developed so far. Amongst them, magnetic nanoparticles (MNPs) have attracted much interest due to the added advantage of facile separation and recovery from reaction media that lowers operating costs compared to traditional methods like filtration and centrifugation [10,11] .…”

Section: Introductionmentioning

confidence: 99%

“…Various reports explain the immobilization of laccase on magnetite nanoparticles (MNPs) via covalent conjugation, co‐entrapment in mesoporous structures, or magnetic hierarchical structures to obtain both activity and magnetic properties [8,12,20] . Although these methods provide improved stability under variable conditions, however, decrease in activity has been found in most of the cases.…”

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Enhanced Laccase Activity and Stability as Crosslinked Enzyme Aggregates on Magnetic Copper Ferrite Nanoparticles for Biotechnological Processes

Escalante Morales,

Sengar,

Dorado Baeza

et al. 2023

ChemCatChem

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Highly stable and reusable magnetic crosslinked enzyme aggregates (m‐CLEAS) of laccase are synthesized with simultaneous improved enzymatic activity. Magnetic copper ferrite nanoparticles (CFNPs) were synthesized by solvothermal procedure with an average size of ~8 nm. The nanometric m‐CLEAS were formed by co‐aggregation of enzyme with CFNPs and crosslinked using glutaraldehyde. Different mass ratios of CFNPs:Laccase were assayed (1:2, 1:3, and 1:6), where 1:6 resulted in the highest activity recovery (97%). The m‐CLEAS showed an average size of ~239 nm, ~24% enzyme immobilization efficiency, and loading as high as 1.75 g of protein per g of support. As expected, m‐CLEAS oxidized the substrate with a higher transformation rate (kcat) and catalytic efficiency (kcat/Km) than the free enzyme. m‐CLEAS showed superior storage and thermostability compared to free enzyme and non‐magnetic CLEAS. In particular, the m‐CLEAS showed ~137% and ~111% residual activity after 30 days of storage at 4˚C and room temperature, respectively. Furthermore, m‐CLEAS showed good recyclability, retaining ~78% and ~54% laccase activity after 5 and 10 cycles of reuse, respectively. This work highlights the facile and cost‐effective synthesis of nanometric m‐CLEAS with exceptional storage stability and simultaneously improved laccase activity, making them suitable for a range of green industrial processes.

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Enhancing enzymatic catalysis efficiency: Immobilizing laccase on HHSS for synergistic bisphenol A adsorption and biodegradation through optimized external surface utilization

Yu,

Feng,

Abbas

et al. 2024

International Journal of Biological Macromolecules

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Immobilization of Aspergillus sp. laccase on hierarchical silica MFI zeolite with embedded macropores

Cited by 6 publications

References 71 publications

Construction of Immobilized Laccase System Based on ZnO and Degradation of Mesotrione

Construction of Immobilized Laccase System Based on ZnO and Degradation of Mesotrione

Enhanced Laccase Activity and Stability as Crosslinked Enzyme Aggregates on Magnetic Copper Ferrite Nanoparticles for Biotechnological Processes

Enhancing enzymatic catalysis efficiency: Immobilizing laccase on HHSS for synergistic bisphenol A adsorption and biodegradation through optimized external surface utilization

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