Polymerization potential of a bacterial CotA-laccase for β-naphthol: enzyme structure and comprehensive polymer characterization DOI Creative Commons

M. Refaat,

Marwa T. ElRakaiby, Mustapha El Hariri El Nokab

et al.

Frontiers in Microbiology, Journal Year: 2024, Volume and Issue: 15

Published: Nov. 21, 2024

Introduction Laccases are blue-multicopper containing enzymes that known to play a role in the bioconversion of recalcitrant compounds. Their free radical polymerization aromatic compounds for their valorization remains underexplored. In this study, we used pBAD plasmid previously characterized CotA laccase gene (abbreviated as Bli -Lacc) from Bacillus licheniformis strain ATCC 9945a express enzyme and explore its biotransformation/polymerization potential on β-naphthol. Methods The protein was expressed TOP10 cells Escherichia coli after successful transformation plasmid. Immobilized metal affinity chromatography (IMAC) generate pure protein. biocatalytic reaction optimized based temperature, pH starting concentration. 1 H 13 C solution nuclear magnetic resonance (NMR), Fourier transform infrared spectroscopy (FTIR), solid-state NMR (ssNMR) were characterize formed polymer. A one-gram conversion done applicability pilot-scale. Results generated brown precipitate, chemical structure confirmed using FTIR. SsNMR revealed presence two different orientational hydroxyl functional groups polymer addition very small amount ether linkages (< 2%). This analysis elucidated occurred mainly carbons rings, rather than attached groups, resulting condensed ring or polynuclear structure. optimized, highest yield attained under conditions 37°C, 10 concentration 440 nM 50 mM phosphate buffer. yielded 216 mg dry mass. crystal solved at 2.7 Å resolution X-ray crystallography presented with hexagonal space group. final deposited Protein Databank (PDB) an ID−9BD5. Discussion article provides green/enzymatic pathway remediation phenolics into useful polymeric materials. comprehensive insight moieties present. Based conversion, synthetic method proves pilot-scale production level opens opportunities invest industrial/environmental applications.

Language: Английский

A novel and sustainable composite of L@PSAC for superior removal of pharmaceuticals from different water matrices: Production, characterization, and application DOI Creative Commons
Osamah J. Al-sareji, Shatha Y. Al-Samarrai, Ruqayah Ali Grmasha

et al.

Environmental Research, Journal Year: 2024, Volume and Issue: 251, P. 118565 - 118565

Published: March 1, 2024

This study endeavors to develop cost-effective environmentally friendly technology for removing harmful residual pharmaceuticals from water and wastewater by utilizing the effective adsorption of pistachio shell (PS) biochar degradation potency laccase immobilized on (L@PSAC). The carbonatization activation shells were optimized regarding temperature, time, NH4NO3/PS ratio. step yielded an optimum PS (PSAC) with highest porosity surface area treated at 700 °C 3 h using ratio 3% wt. immobilization onto PSAC (L@PSAC) was its best level pH 5, 60 U/g, 30 °C. L@PSAC maintained a high enzyme activity over two months. Almost complete removal (>99%) diclofenac, carbamazepine, ciprofloxacin in Milli-Q (MQ) achieved. Adsorption responsible >80% rest facilitated degradation. ≥60% up six treatment cycles underscoring promising application this material treatment. These results indicate that activated carbon derived could potentially be utilized as carrier adsorbent efficiently remove pharmaceutical compounds. enzymatic physical elimination approach has potential used large-scale.

Language: Английский

Citations

11

Development of a robust enzyme cascade system: co-immobilization of laccase and versatile peroxidase on polyacrylamide hydrogel for enhanced BPA degradation DOI
Shagufta Kamal,

Taleeha Roheen,

Kanwal Rehman

et al.

Biodegradation, Journal Year: 2025, Volume and Issue: 36(3)

Published: April 21, 2025

Language: Английский

Citations

0

Effects of modified bentonites immobilized crude enzymes on soil properties and microbial community of BaP contaminated soil DOI
Dawen Gao, Guanyu Chen, Zelin Hou

et al.

Journal of environmental chemical engineering, Journal Year: 2025, Volume and Issue: unknown, P. 116574 - 116574

Published: April 1, 2025

Language: Английский

Citations

0

Immobilization of fungal laccase on peanut shell carriers DOI
María Pilar Serbent, María Daniela Rodríguez, Clara Saux

et al.

Biocatalysis and Agricultural Biotechnology, Journal Year: 2025, Volume and Issue: unknown, P. 103581 - 103581

Published: April 1, 2025

Language: Английский

Citations

0

Enhancing Laccase Production by Trametes hirsuta GMA-01 Using Response Surface Methodology and Orange Waste: A Novel Breakthrough in Sugarcane Bagasse Saccharification and Synthetic Dye Decolorization DOI Creative Commons

Guilherme Guimarães Ortolan,

Alex Graça Contato, Guilherme Mauro Aranha

et al.

Reactions, Journal Year: 2024, Volume and Issue: 5(3), P. 635 - 650

Published: Sept. 19, 2024

Trametes hirsuta GMA-01 was cultivated in a culture medium supplemented with orange waste, starch, wheat bran, yeast extract, and salts. The fungus produced several holoenzymes, but the laccase levels were surprisingly high. Given highlighted applicability of laccases various biotechnological areas minimal environmental impact, we provided strategy to increase its production using response surface methodology. immobilization into ionic supports (CM-cellulose, DEAE-agarose, DEAE-cellulose, DEAE-Sephacel, MANAE-agarose, MANAE-cellulose, PEI-agarose) found be efficient recuperative, showcasing technical prowess research. crude extract (CE) CM-cellulose-immobilized (ICE) showed optimum activity acidic conditions (pH 3.0) at 70 °C for CE 60 ICE. ICE significantly increased thermostability which retained 21.6% residual after 240 min. successfully applied sugarcane bagasse hydrolysis, showing 13.83 ± 0.02 µmol mL−1 reducing sugars 48 h. Furthermore, tested dye decolorization, achieving 96.6%, 71.9%, 70.8% decolorization bromocresol green, bromophenol blue, orcein, respectively (0.05% (w/v) concentration). properties versatility T. different purposes are interesting notable, opening potential applications providing valuable insights future development.

Language: Английский

Citations

1

Polysaccharides and Composite Adsorbents in the Spotlight for Effective Agrochemical Residue Removal from Water DOI Creative Commons
Mónica Ortiz‐Martínez,

Brenda Restori-Corona,

Luis Hernández-García

et al.

Macromol—A Journal of Macromolecular Research, Journal Year: 2024, Volume and Issue: 4(4), P. 785 - 804

Published: Nov. 6, 2024

Agrochemical residues, including pesticides and herbicides, pose significant environmental health risks when present in water sources. Conventional treatment methods often fall short effectively removing these persistent pollutants, necessitating innovative solutions. This review explores the use of polysaccharides composite adsorbents as sustainable alternatives for agrochemical residue removal from water. Biopolymers such chitosan, alginate, cellulose are highlighted their biodegradability, biocompatibility, ability to be functionalized enhanced adsorption performance. Recent advances development materials incorporating nanomaterials, graphene, oxide, metal oxides, have shown promise enhancing efficiency selectivity adsorption. The also addresses fundamental mechanism adsorption, electrostatic interactions, hydrogen bonding, hydrophobic forces, that contribute effectiveness materials. Challenges associated with scalability, regeneration, real-world applications discussed, well future opportunities integrating emerging technologies like 3D printing machine learning into adsorbent design. Overall, composites offer a promising pathway toward achieving efficient removal, ongoing research needed overcome current limitations optimize practical application treatment.

Language: Английский

Citations

1

Enhanced Thermostability of Laccase from Myceliophthora thermophila Through Conjugation with mPEG-SC DOI Open Access
Lorena Garcı́a,

Raissa H. S. Florindo,

Vivian Sáez

et al.

Catalysts, Journal Year: 2024, Volume and Issue: 14(12), P. 887 - 887

Published: Dec. 3, 2024

The search for more sustainable reaction conditions has been necessary to obtain selective processes. In this context, laccases have gained great notoriety in recent years. However, these enzymes are unstable organic solvents and low thermal stability. Alternatively, conjugation with PEG (PEGylation) can be essential overcome problems. work, the commercial laccase from Myceliophthora thermophila (LacMT) was subjected PEGylation functionalized as succinimidyl carbonate (mPEG-SC), followed by assessing its stability catalytic activity. Mono-PEGylated LacMT derivatives were obtained, less than 50% of enzyme remaining native form. addition, 10% bi-PEGylated species successfully obtained according gel electrophoresis analysis. PEGylated showed a significantly reduced ABTS oxidation activity (98 ± 3 U/mg) compared (407 9 but higher control without (51 2 U/mg), demonstrating that addition activated protein resulted better protection against harmful action pH change required process. retained twice initial at 40 °C during 24 h. exhibited kinetic changes, whereas turnover rate (kcat) 27% control. These findings being reported first time. This sets precedents constructing efficient systems involving since no immobilized biocatalyst or conjugate contains proteins.

Language: Английский

Citations

0

Polymerization potential of a bacterial CotA-laccase for β-naphthol: enzyme structure and comprehensive polymer characterization DOI Creative Commons

M. Refaat,

Marwa T. ElRakaiby, Mustapha El Hariri El Nokab

et al.

Frontiers in Microbiology, Journal Year: 2024, Volume and Issue: 15

Published: Nov. 21, 2024

Introduction Laccases are blue-multicopper containing enzymes that known to play a role in the bioconversion of recalcitrant compounds. Their free radical polymerization aromatic compounds for their valorization remains underexplored. In this study, we used pBAD plasmid previously characterized CotA laccase gene (abbreviated as Bli -Lacc) from Bacillus licheniformis strain ATCC 9945a express enzyme and explore its biotransformation/polymerization potential on β-naphthol. Methods The protein was expressed TOP10 cells Escherichia coli after successful transformation plasmid. Immobilized metal affinity chromatography (IMAC) generate pure protein. biocatalytic reaction optimized based temperature, pH starting concentration. 1 H 13 C solution nuclear magnetic resonance (NMR), Fourier transform infrared spectroscopy (FTIR), solid-state NMR (ssNMR) were characterize formed polymer. A one-gram conversion done applicability pilot-scale. Results generated brown precipitate, chemical structure confirmed using FTIR. SsNMR revealed presence two different orientational hydroxyl functional groups polymer addition very small amount ether linkages (< 2%). This analysis elucidated occurred mainly carbons rings, rather than attached groups, resulting condensed ring or polynuclear structure. optimized, highest yield attained under conditions 37°C, 10 concentration 440 nM 50 mM phosphate buffer. yielded 216 mg dry mass. crystal solved at 2.7 Å resolution X-ray crystallography presented with hexagonal space group. final deposited Protein Databank (PDB) an ID−9BD5. Discussion article provides green/enzymatic pathway remediation phenolics into useful polymeric materials. comprehensive insight moieties present. Based conversion, synthetic method proves pilot-scale production level opens opportunities invest industrial/environmental applications.

Language: Английский

Citations

0