The Immobilization of Laccase on Mixed Polymeric Microspheres for Methyl Red Decomposition

Aricov, Ludmila; Răducan, Adina; Gîfu, Ioana Cătălina; Alexandrescu, Elvira; Precupaş, Aurica; Neculae, Alexandru Vincentiu Florian; Visan, Raluca M; Moroșan, Alina; Leontieş, Anca Ruxandra

doi:10.3390/coatings12121965

Cited by 6 publications

(1 citation statement)

References 58 publications

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“…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%

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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Section: Introductionmentioning

confidence: 99%

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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“In Silico” prediction of antibiotics biodegradation by Ganoderma lucidum GILCC 1 laccase

Mora-Gamboa,

Ardila-Leal,

Galindo

et al. 2024

Discov Appl Sci

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Antibiotics present a pressing environmental challenge as emerging pollutants due to their persistence and role in promoting antibiotic-resistant bacteria. To model the utilization of Ganoderma lucidum GlLCC1 laccase in degrading antibiotics, a 3D homology model of GILCC1, based on Lentinus tigrinus mushroom laccase, was utilized. Five broad-spectrum WHO-designated antibiotics with molecular weights between 100 and 500 Da were selected. Molecular dynamics simulations were conducted at pH 3.0 and 7.0 to evaluate the interactions between GILCC1 and antibiotics in a TIP3P water box, with system behaviour assessed at 300 °K using an NPT assembly. ABTS (2,2ʹ-Azino-bis (3-ethylbenzthiazoline-6-sulfonic Acid)) served as the comparison molecule. The binding free energy indicated a strong affinity between 3D GILCC1 and various ligands. At pH 3.0, GILCC1 exhibited significant Gibbs free energy (ΔG), indicating a high affinity for Levofloxacin (LVX; −8.2 kcal mol−1), Sulfisoxazole (SFX; −7.8 kcal mol−1), Cefuroxime (CXM; −7.5 kcal mol−1), Cephradine (CFD; −7. 5 kcal mol−1), ABTS (−7.6 kcal mol−1), and Tetracycline (TE; −7.5 kcal mol−1), attributed to pocket topology and interactions such as hydrogen bonds and van der Waals forces. Electron transfer in GILCC1 involved a chain of residues, including His395 and Phe239. Although the affinity decreased at pH 7.0, the potential of GILCC1 to degrade antibiotics remained plausible. This study accurately predicted the behaviour of the laccase-antibiotic system, providing atomic-level insights into molecular interactions and emphasizing the importance of experimental assays and assessments of antibiotic degradation in wastewater, considering various chemical compounds. The use of ABTS as a mediator was suggested to enhance molecule affinity. Graphical abstract

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Trametes versicolor laccase activity modulated by the interaction with gold nanoparticles

Aricov,

Precupas,

Tudose

et al. 2023

Environmental Research

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The Immobilization of Laccase on Mixed Polymeric Microspheres for Methyl Red Decomposition

Cited by 6 publications

References 58 publications

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

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

“In Silico” prediction of antibiotics biodegradation by Ganoderma lucidum GILCC 1 laccase

Trametes versicolor laccase activity modulated by the interaction with gold nanoparticles

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