Co-immobilization of lipase and laccase on agarose-based supports via layer-by-layer strategy: Effect of diffusional limitations

Santos, Kimberle Paiva dos; Rios, Nathália Saraiva; Labus, Karolina; Gonçalves, Luciana Rocha Barros

doi:10.1016/j.bej.2022.108533

Cited by 9 publications

(4 citation statements)

References 68 publications

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“…Such variation in kinetic parameters has been observed in other studies. For example, Dos Santos et al [43] co-immobilized laccase on agarose-based supports and found a similar trend to that identified in the present work; the Vmax values of the laccase showed a slight decrease upon immobilization (around 0.13 mM/min), but the values of Km did not significantly change (around 0.04 mM). Ruqayah et al [38] immobilized laccase on modified multiwall carbon nanotubes.…”

Section: Kinetic Parameterssupporting

confidence: 90%

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: Kinetic Parameterssupporting

confidence: 90%

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

Yue,

Wang,

Zhang

et al. 2024

Toxics

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“…The Michaelis-Menten curve of the immobilized enzyme showed substrate inhibition at a high concentration of ABTS. 64 The same phenomenon was observed by Dos Santos et al 60 It could be possible that ABTS is not totally removed from the biocatalyst after the first reuse cycle leading to an ABTS accumulation that inhibits the laccase activity as a consequence of a rapid LC@ZMFI inactivation.…”

Section: Storage Stability and Reuse Of Lc@zmfisupporting

confidence: 53%

“…The kinetic parameters regarding of the laccase showed a slight decrease upon immobilization from 0.072 to 0.068 and 0.21 to 0.13 for KM and Vmax respectively. 60 Ameri et al reported the immobilization by physical adsorption of laccase from Trametes versicolor onto two hierarchical zeolites called HR-Y and HR-Z. They obtained a Vmax of 1.11 and 1.02 μmol min -1 and a KM of 0.26 and 0.31 mM for HR-Y and HR-Z, respectively.…”

Section: Wang Et Al 58mentioning

confidence: 99%

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

Tocco

Wisser

Fischer

et al. 2023

Colloids and Surfaces B: Biointerfaces

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“…"Immobilized enzymes," BioResources 18(4), Pg#s to be added. 14 important to increase porosity or immobilize on non-porous supports (Bourkaib et al 2021;Santos et al 2022b). Compared with the yield of reducing sugars obtained after the hydrolysis of microcrystalline cellulose, the yield was increased by 133% when utilizing the support with PEG compared to immobilizing cellulase with the one without the treatment.…”

Section: Fig 2 Diffusional Effects On Enzymes Immobilized By Substrat...mentioning

confidence: 99%

Enzyme technology in bioethanol production from lignocellulosic biomass: Recent trends with a focus on immobilized enzymes

de Araújo,

Costa,

de Brito

et al. 2023

BioRes

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Enzyme immobilization is a useful tool to produce biocatalysts with improved performance, such as high activity, high stability at operational conditions, and easy recovery and reuse. In this context, the production of second-generation ethanol using immobilized enzymes was reviewed. Emphasis was placed on the pre-treatment and/or hydrolysis steps to increase efficiency and reduce the cost of the process. In addition, the process design of bioethanol using immobilized enzymes was critically reviewed. In the enzymatic pre-treatment, laccases, manganese peroxidases, lignin peroxidases, and lytic polysaccharide monooxygenases are the main enzymes involved. When considering processes with heterogeneous biocatalysts, laccases are the most explored enzyme. In the hydrolysis step, cellulases and hemicellulases or a mixture of them are the main enzymes explored in the literature frequently using magnetic nanoparticles as support for enzyme immobilization. Although enzyme immobilization is a mature technology, the use of these biocatalysts is frequently limited to only one step of the bioethanol production process, such as pre-treatment or hydrolysis performed using Benchmark Technology. However, some recent papers have explored innovative design processes using a mixture of immobilized enzymes or co-immobilized enzymes to join some process steps, thereby decreasing the cost of enzymes and equipment.

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Co-immobilization of lipase and laccase on agarose-based supports via layer-by-layer strategy: Effect of diffusional limitations

Cited by 9 publications

References 68 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

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

Enzyme technology in bioethanol production from lignocellulosic biomass: Recent trends with a focus on immobilized enzymes

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