Enzymatic route for selective glycerol oxidation using covalently immobilized laccases

Bîtcan, Ioan; Petrovici, Andreea; Pellis, Alessandro; Klébert, Szilvia; Károly, Zoltán; Bereczki, Laura; Péter, Fráncisc; Todea, Anamaria

doi:10.1016/j.enzmictec.2022.110168

Cited by 6 publications

(2 citation statements)

References 61 publications

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“…In this contest, for selective glycerol oxidation via enzymatic route, Bîtcan has reported how laccases from Trametes versicolor and Aspergillus sp. were immobilized by covalent binding onto magnetic particles, which were previously functionalized by using 3‐aminopropyl‐trimethoxysilane (NH 2 ‐TMOS) or 3‐aminopropyl‐triethoxysilane (NH 2 ‐TEOS) and activated with glutaraldehyde (Bîtcan et al., 2023).…”

Section: Immobilizationmentioning

confidence: 99%

Biocatalyst immobilization on magnetic nano‐architectures for potential applications in condensation reactions

Papatola,

Slimani,

Peddis

et al. 2024

Microbial Biotechnology

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In this review article, a perspective on the immobilization of various hydrolytic enzymes onto magnetic nanoparticles for synthetic organic chemistry applications is presented. After a first part giving short overview on nanomagnetism and highlighting advantages and disadvantages of immobilizing enzymes on magnetic nanoparticles (MNPs), the most important hydrolytic enzymes and their applications were summarized. A section reviewing the immobilization techniques with a particular focus on supporting enzymes on MNPs introduces the reader to the final chapter describing synthetic organic chemistry applications of small molecules (flavour esters) and polymers (polyesters and polyamides). Finally, the conclusion and perspective section gives the author's personal view on further research discussing the new idea of a synergistic rational design of the magnetic and biocatalytic component to produce novel magnetic nano‐architectures.

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Section: Immobilizationmentioning

confidence: 99%

Biocatalyst immobilization on magnetic nano‐architectures for potential applications in condensation reactions

Papatola,

Slimani,

Peddis

et al. 2024

Microbial Biotechnology

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“…Under similar recycling conditions, Fe 3 O 4 /Mn-TvLac retained much better residual activities of 98.7% and 96.8%, respectively. Under various recycling conditions, an immobilized system based on purified laccase exhibited residual activities of (i) ~50% after 10 cycles for Co-based, and dendrimergrafted silica-coated hercynite-copper phosphate magnetic NFs [39,47], (ii) 25-40% after five cycles for ferrite microparticles based on Ni-Zn and Ni-Zn-Co [49], (iii) 30% after 10 cycles for Cu-based NFs [45], and (iv) 40% after 12 cycles for Zn-based NFs [41]. During the reusability test, successive decreases in the immobilized laccase residual activity of Mn-TvLac can be linked to the leaching of bound enzymes or their inactivation due to the deformation of the NF matrix [18,40].…”

Section: Temperature (°C)mentioning

confidence: 99%

Trametes versicolor Laccase-Based Magnetic Inorganic-Protein Hybrid Nanobiocatalyst for Efficient Decolorization of Dyes in the Presence of Inhibitors

Patel,

Gupta,

Karuppanan

et al. 2024

Materials

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In the present investigation, an ecofriendly magnetic inorganic-protein hybrid system-based enzyme immobilization was developed using partially purified laccase from Trametes versicolor (TvLac), Fe3O4 nanoparticles, and manganese (Mn), and was successfully applied for synthetic dye decolorization in the presence of enzyme inhibitors. After the partial purification of crude TvLac, the specific enzyme activity reached 212 U∙mg total protein−1. The synthesized Fe3O4/Mn3(PO4)2-laccase (Fe3O4/Mn-TvLac) and Mn3(PO4)2-laccase (Mn-TvLac) nanoflowers (NFs) exhibited encapsulation yields of 85.5% and 90.3%, respectively, with relative activities of 245% and 260%, respectively, compared with those of free TvLac. One-pot synthesized Fe3O4/Mn-TvLac exhibited significant improvements in catalytic properties and stability compared to those of the free enzyme. Fe3O4/Mn-TvLac retained a significantly higher residual activity of 96.8% over that of Mn-TvLac (47.1%) after 10 reuse cycles. The NFs showed potential for the efficient decolorization of synthetic dyes in the presence of enzyme inhibitors. For up to five reuse cycles, Fe3O4/Mn-TvLac retained a decolorization potential of 81.1% and 86.3% for Coomassie Brilliant Blue R-250 and xylene cyanol, respectively. The synthesized Fe3O4/Mn-TvLac showed a lower acute toxicity towards Vibrio fischeri than pure Fe3O4 nanoparticles did. This is the first report of the one-pot synthesis of biofriendly magnetic protein-inorganic hybrids using partially purified TvLac and Mn.

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Electrocatalytic oxidation of glycerol performed by nickel/cobalt alloys: Adding value to a common subproduct of chemical industry

Massaneiro,

Valério,

Pellosi

et al. 2024

Electrochimica Acta

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Enzymatic route for selective glycerol oxidation using covalently immobilized laccases

Cited by 6 publications

References 61 publications

Biocatalyst immobilization on magnetic nano‐architectures for potential applications in condensation reactions

Biocatalyst immobilization on magnetic nano‐architectures for potential applications in condensation reactions

Trametes versicolor Laccase-Based Magnetic Inorganic-Protein Hybrid Nanobiocatalyst for Efficient Decolorization of Dyes in the Presence of Inhibitors

Electrocatalytic oxidation of glycerol performed by nickel/cobalt alloys: Adding value to a common subproduct of chemical industry

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