Immobilized laccase on zinc oxide nanoarray for catalytic degradation of tertiary butyl alcohol

Isanapong, Jantiya; Pornwongthong, Peerapong

doi:10.1016/j.jhazmat.2021.125104

Cited by 27 publications

(10 citation statements)

References 53 publications

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“…Various inorganic and organic nanomaterials such as silica nanoparticles [ 593 ], Manganese ferrite nanoparticles [ 594 ], copper ferrite nanoparticles [ 595 ], Titanium oxide nanoparticles [ 256 ], Halloysite nanotubes (HNTs) [ 178 , 295 ], Graphene nanosheets [ 110 ], ZnO nanoparticles [ 596 ], carbon nanotubes and nanospheres [ 206 , 310 , 415 ], gold nanoparticles, and metal oxide nanoparticles have been used as carriers to immobilize enzymes. The advantages associated with immobilizing enzymes on nanomaterials are: they provide high surface area for enzyme attachment and high effective enzyme loading, high mechanical resistance, and their similar size to enzymes ensures minimal diffusion limitations and a reduced mass transfer resistance [ 75 , 192 , 597 ].…”

Section: Supports Used For Laccase Immobilizationmentioning

confidence: 99%

Applications and immobilization strategies of the copper-centred laccase enzyme; a review

Kyomuhimbo¹,

Brink²

2023

Heliyon

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Section: Supports Used For Laccase Immobilizationmentioning

confidence: 99%

Applications and immobilization strategies of the copper-centred laccase enzyme; a review

Kyomuhimbo¹,

Brink²

2023

Heliyon

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“…The K m value indicated that the free alginate lyase was more sensitive to the substrate than that of the immobilized alginate lyase. This is because the spatial structure and active site of the enzyme molecules were changed after immobilization [41,42]. The immobilized alginate lyase formed a certain steric hindrance which hindered the contact between the enzyme molecules and the substrate molecules.…”

Section: The Thermal Stabilitymentioning

confidence: 99%

Preparation, structural characterization and enzymatic properties of alginate lyase immobilized on magnetic chitosan microspheres

Li,

Yan,

Huang

et al. 2023

Preprint

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Alginate lyase is an enzyme that catalyzes the hydrolysis of alginate into alginate oligoalginates. To enhance enzyme stability and recovery, a facile strategy for alginate lyase immobilization was developed. The novel magnetic chitosan microspheres were synthesized and used as a carrier to immobilize alginate lyase. Immobilization of alginate lyase on magnetic chitosan microspheres was successful as proved by the Fourier transform infrared spectroscopy and X-ray diffraction spectra. The enzyme immobilization exhibited best performance at MCM dosage = 1.5 g/L, adsorption time = 2.0 h, glutaraldehyde concentration = 0.2%, and immobilization time = 2.0 h. The optimal pH of the free alginate lyase was 7.5, and this pH value was shifted to 8.0 after immobilization. No difference was observed in the optimal temperature (45°C) for the immobilized and free enzymes. The immobilized alginate lyase displayed superior thermal stability compared with the free alginate lyase. The Km of the free and immobilized enzymes were 0.05 mol/L and 0.09 mol/L, respectively. The immobilized alginate lyase retained 72% of its original activity after 10 batch reactions. This strategy was a promising method to immobilize alginate lyase.

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“…Because of their excellent biocompatibility, chemical stability, and non-toxicity, ZnO nanomaterials have been widely used as chemical sensors and antibacterial agents, as well as for environmental applications [ 28 , 29 , 30 ]. Jantiya Isanapong et al [ 31 ] evaluated the efficiency of immobilized laccase for the degradation of tertiary butyl alcohol (TBA) on ZnO nanostructures; they found that immobilized laccase exhibited better stability and degradation. Manviri Rani et al [ 32 ] prepared lac-ZnO nanospheres and found that they exhibited improved enzymatic properties compared with free laccase.…”

Section: Introductionmentioning

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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Immobilized laccase on zinc oxide nanoarray for catalytic degradation of tertiary butyl alcohol

Cited by 27 publications

References 53 publications

Applications and immobilization strategies of the copper-centred laccase enzyme; a review

Applications and immobilization strategies of the copper-centred laccase enzyme; a review

Preparation, structural characterization and enzymatic properties of alginate lyase immobilized on magnetic chitosan microspheres

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

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