Preparation and synthetic dye decolorization ability of magnetic cross-linked enzyme aggregates of laccase from Bacillus amyloliquefaciens

Wang, Hongrao; Han, Shuran; Wang, Jiayi; Yu, Shuyu; Li, Xiaoyan; Lu, Lei

doi:10.1007/s00449-020-02481-8

Cited by 12 publications

(11 citation statements)

References 31 publications

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“…Wang et al observed an opposite trend where increasing the mass ratio of MNPs to laccase showed higher activity. [27] On the other hand, Muthuvelu et al analyzed the effect of Cu 2 + ion concentration on the activity of laccase, and 15 mM CuSO4 was found to increase the relative activity by 16 %, while at higher concentrations, the activity decreased. [13] Thus, it is anticipated that 1 : 6 mass ratio of CFNPs:Laccase provides an appropriate copper ions concentration for the activity enhancement.…”

Section: Synthesis and Characterization Of Cleas And M-cleasmentioning

confidence: 99%

“…[25] While other reports mentioned decreased laccase activity after immobilization on MNPs as m-CLEAS. [24,[26][27][28] However, these values should be taken cautiously because they are highly dependent on the conditions in which the enzymatic reactions were evaluated.…”

Section: Kinetic Constantsmentioning

confidence: 99%

“…The increase in thermostability can be attributed to the higher rigidity obtained after enzyme immobilization by cross-linking. [19,25,27] pH activity profile…”

Section: Thermal Stabilitymentioning

confidence: 99%

“…[23] While m-CLEAS of laccase were synthesized using amine-functionalized magnetite nanoparticles with improved stability and recyclability for application in wastewater treatment and dye discoloration. [24][25][26][27] Recently, a comparative analysis of CLEAS and m-CLEAS of different enzymes, including laccase on maghemite nanoparticles, was performed, highlighting the better stability of m-CLEAS. [28] In this work, m-CLEAS of laccase of Coriolopsis gallica are synthesized using CFNPs as magnetic core and analyzed for catalytic activity, stability at variable conditions, and recyclability for its potential application in industrial biotechnological processes.…”

Section: Introductionmentioning

confidence: 99%

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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: Synthesis and Characterization Of Cleas And M-cleasmentioning

confidence: 99%

Section: Kinetic Constantsmentioning

confidence: 99%

“…The increase in thermostability can be attributed to the higher rigidity obtained after enzyme immobilization by cross-linking. [19,25,27] pH activity profile…”

Section: Thermal Stabilitymentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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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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“…Industrial application of mCLEAs and m-combi-CLEAs has the possibility of using them in the complex conversions of polysaccharides such as starch (Torabizadeh and Montazeri, 2020), lignocellulose for the production of firstand second-generation biofuels (Cruz-Izquierdo et al, 2015), for the synthesis of bioactive molecules as aglycone (Wei et al, 2022), and for clarification and flavor enhancers in food and beverages (Dal Magro et al, 2018). Likewise, magnetic CLEAs can be used in the conversion of biomass as in the valorization of keratin-rich poultry industry wastes where keratinase m-CLEA showed enhanced activity and stability than the soluble enzyme (Lotfi et al, 2021), as well as in the enantioselective reduction of prochiral ketones catalyzed by magnetic combi-CLEAs of his-tagged ketoreductase and histagged glucose oxidase (Peschke et al, 2019), for dyedegradation in wastewater (Wang et al, 2021). New CLEAs for industrial applications have gained prominence in this context since they generate correct environmental products and sustainable chemical systems.…”

mentioning

confidence: 99%

Editorial: Designing Carrier-Free Immobilized Enzymes for Biocatalysis

Velasco‐Lozano

Rocha-Martín

Santos

2022

Front. Bioeng. Biotechnol.

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Editorial on the Research TopicDesigning Carrier-free Immobilized Enzymes for Biocatalysis Global challenges in energy, resources, environment and sustainable chemical processing are leading us to minimize the use of natural resources, toxic materials, energy, and the generation of waste and pollutants. Enzymatic biocatalysis development evolves to strengthen the ongoing required process improvements of current industrial chemical transformations, where enzymes are naturally available, efficient biocatalysts exhibiting high specificity and enantioselectivity. However, for their industrial application, enzymes must possess high stability under large-scale producing conditions (such as high substrate and product concentrations, temperature, presence of solvents), where enzymes easily become inactive due to their low stability under such unnatural conditions or the almost null activity toward non-natural substrates. In this context, enzyme immobilization is a strategy that can facilitate their stabilization, purification, and reuse in the industry (Cavalcante et al., 2021; da S. Moreira et al., 2021;Reis et al., 2019). Enzymes can be immobilized on water-insoluble supports or without supports. Among carrier-free immobilization methods, the Cross-Linked Enzyme Aggregates (CLEA) emerged as a promising technology capable of manufacturing robust immobilized protein aggregates. In general, the preparation of CLEA involves the first stage of precipitation of enzymatic molecules followed by a cross-linking step managed by the action of a bifunctional reagent added to the reaction system, the cross-linker. As a result, the aggregates become insoluble, maintaining high catalytic activity, excellent stability, and low production cost.Another possibility of immobilizing enzymes free of support is the cross-linked enzyme crystals (CLEC). Compared to soluble enzymes, CLEC is more robust, controllable in size, resistant to organic solvents, and inactivates by heat or proteolysis. However, in contrast with CLEA, CLEC requires purified enzymes to achieve the required enzyme crystals formation, thus hampering their implementation at significant scale processes.CLEAs's physical and catalytic properties are strongly influenced and controlled through the preparation process (Table 1). Several works have summarized the most reported variables leading to robust CLEA biocatalysts from a wide variety of different enzymes, such as hydrolases, oxidoreductases, lyases, transferases, and isomerases for different industrial applications (Talekar

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In situ encapsulation of laccase in mesoporous amorphous ZIF‐8 for Reactive Blue 19 removal

Shi

Xing

Gong

et al. 2023

Water Environment Research

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Laccase with substrate non‐specificity is particularly effective in pollutant degradation. However, the practical application of the laccase is limited due to its poor stability and reusability. In this study, a simple in situ encapsulation method was used to immobilize laccase into amorphous zeolitic imidazolate frameworks‐8 (aZIF‐8), and the synthesized Lac@aZIF‐8 biocomposites were used to remove Reactive Blue 19 (RB 19). Results indicated that the presence of mesoporous endowed the immobilized laccase with higher substrate affinity. Compared with free laccase, the Lac@aZIF‐8 showed higher thermo‐tolerant performance, wider pH range, better storage stability, and reusability. The Lac@aZIF‐8 biocomposites have excellent performance in the effective removal of RB 19. Without any mediators, the dye decolorization rate of immobilized laccase reached up to 82% in 3 h under optimal conditions. Based on the LC‐MS analysis, the proposed degradation pathways of RB 19 were discussed technically. Moreover, the growth inhibition experiments on Scenedesmus obliquus confirmed the lower toxicity intensity of the degradation products. This research enhanced the stability of laccase while maintaining high substrate affinity, providing a novel strategy for the green and efficient treatment of dye wastewater. Practitioners Points Lac@aZIF‐8 was synthesized by a simple in situ encapsulation method. The mesoporous structure endows the immobilized laccase with higher substrate affinity. The Lac@aZIF‐8 shows higher thermo‐tolerant performance, wider pH range, better storage stability, and reusability. The Lac@aZIF‐8 biocomposites have excellent performance in RB 19 removal.

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Preparation and synthetic dye decolorization ability of magnetic cross-linked enzyme aggregates of laccase from Bacillus amyloliquefaciens

Cited by 12 publications

References 31 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

Editorial: Designing Carrier-Free Immobilized Enzymes for Biocatalysis

In situ encapsulation of laccase in mesoporous amorphous ZIF‐8 for Reactive Blue 19 removal

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