Immobilization of laccase on magnetic nanoparticles for enhanced polymerization of phenols.
Laccase immobilization
Magnetic nanoparticle
Phenol polymerization
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
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
110331Informations 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.