Immobilization of laccase on magnetic nanoparticles for enhanced polymerization of phenols.


Journal

Enzyme and microbial technology
ISSN: 1879-0909
Titre abrégé: Enzyme Microb Technol
Pays: United States
ID NLM: 8003761

Informations de publication

Date de publication:
Jan 2024
Historique:
received: 06 06 2023
revised: 18 09 2023
accepted: 03 10 2023
medline: 20 11 2023
pubmed: 16 10 2023
entrez: 15 10 2023
Statut: ppublish

Résumé

Laccase is an efficient biocatalyst for oxidative polymerization of organic substrates. However, cost of enzyme preparation, low stability and residual protein diminish the efficiency of laccase mediated polymerization. In this work, a series of silicon dioxide coated ferroferric oxide magnetic nanoparticles were modified by different functional groups including γ-methacryloxypropyltrimethoxy, succinic anhydride, glutaraldehyde and polyethylene imine. Infrared spectra indicated the magnetic carriers have been successfully modified. Vibrating sample magnetometer (VSM) analysis revealed that all of these carriers showed high magnetic responsiveness after the surface functionalization. Laccase from Cerrena sp. HYB07 was then respectively immobilized covalently on these functionalized magnetic carriers. All the immobilized laccases displayed higher thermostability than free laccase and glutaraldehyde functionalized support (named FSNG) immobilized laccase showed better performance. These immobilized laccases all showed higher efficiency than free laccase for oxidative polymerization of catechol and hydroquinone. The immobilized laccases could be separated from the water insoluble polymerization products. The polymerization product of hydroquinone by FSNG immobilized laccase showed the average polymerization degree of the poly(hydroquinone) was six (DP=6). This work provided a comprehensive exploration of laccase immobilization on magnetic carrier for catalyzing polymerization of phenols.

Identifiants

pubmed: 37839253
pii: S0141-0229(23)00139-4
doi: 10.1016/j.enzmictec.2023.110331
pii:
doi:

Substances chimiques

Enzymes, Immobilized 0
Phenols 0
Laccase EC 1.10.3.2
hydroquinone XV74C1N1AE
Hydroquinones 0
Magnetite Nanoparticles 0
Glutaral T3C89M417N

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

110331

Informations de copyright

Copyright © 2023 Elsevier Inc. All rights reserved.

Déclaration de conflit d'intérêts

Declaration of Competing Interest The authors declare that they have no conflict of interest.

Auteurs

Xinqi Xu (X)

College of Biological Science and Engineering, Fuzhou University, Fuzhou 350108, China.

Tianheng Chen (T)

College of Biological Science and Engineering, Fuzhou University, Fuzhou 350108, China.

Lian Xu (L)

College of Biological Science and Engineering, Fuzhou University, Fuzhou 350108, China. Electronic address: xulian@fzu.edu.cn.

Juan Lin (J)

College of Biological Science and Engineering, Fuzhou University, Fuzhou 350108, China. Electronic address: ljuan@fzu.edu.cn.

Articles similaires

Aspergillus Hydrogen-Ion Concentration Coculture Techniques Secondary Metabolism Streptomyces rimosus
Sorghum Antioxidants Phosphorus Fertilizers Flavonoids

Aminoacid functionalised magnetite nanoparticles Fe

Spoială Angela, Motelica Ludmila, Ilie Cornelia-Ioana et al.
1.00
Magnetite Nanoparticles Tryptophan Biocompatible Materials Microbial Sensitivity Tests Humans
Soil Charcoal Nutrients Manure Nitrogen

Classifications MeSH