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1.
Bioprocess Biosyst Eng ; 46(11): 1513-1531, 2023 Nov.
Artigo em Inglês | MEDLINE | ID: mdl-37458833

RESUMO

The bio-enzyme degradation technology is a promising approach to sustainably remove pollution in the water and laccase is one of the most widely used enzymes in this area. Nevertheless, the further industrial application of laccase is limited by low stability, short service, low reusability and high price. The immobilization technology can significantly improve the stability and reusability of enzymes and thus promoting their industrial applications. Nanocomposite materials have been developed and applied in the efficient immobilization of laccase due to their superior physical, chemical, and biological performance. This paper presents a comprehensive review of various nanocomposite immobilization methods for laccase and the consequent changes in enzymatic properties post-immobilization. Additionally, a comprehensive analysis is conducted on the factors that impact laccase immobilization and its water removal efficiency. Furthermore, this review examines the effectiveness of common contaminants' removal mechanisms while summarizing and discussing issues related to laccase immobilization on nanocomposite carriers. This review aims to provide valuable guidance for enhancing laccase immobilization efficiency and enzymatic water pollutant removal.


Assuntos
Poluentes Ambientais , Nanocompostos , Poluentes Químicos da Água , Águas Residuárias , Lacase/química , Enzimas Imobilizadas/química , Água , Poluentes Químicos da Água/metabolismo
2.
Molecules ; 27(23)2022 Dec 03.
Artigo em Inglês | MEDLINE | ID: mdl-36500612

RESUMO

In this study, polyethyleneimine was combined with magnetic Fe3O4 nanoparticles through the bridging of carboxyl-functionalized ionic liquid, and laccase was loaded onto the carrier by Cu2+ chelation to achieve laccase immobilization (MCIL-PEI-Cu-lac). The carrier was characterized by Fourier transform infrared spectroscopy, scanning electron microscope, thermogravimetric analysis, X-ray diffraction analysis, magnetic hysteresis loop and so on. MCIL-PEI-Cu-lac has good immobilization ability; its loading and activity retention could reach 52.19 mg/g and 91.65%, respectively. Compared with free laccase, its thermal stability and storage stability have been significantly improved, as well. After 6 h of storage at 60 °C, 51.45% of the laccase activity could still be retained, and 81.13% of the laccase activity remained after 1 month of storage at 3 °C. In the pollutants removal test, the removal rate of 2,4-dichlorophenol (10 mg/L) by MCIL-PEI-Cu-lac could reach 100% within 10 h, and the removal efficiency could still be maintained 60.21% after repeated use for 8 times. In addition, MCIL-PEI-Cu-lac also has a good removal effect on other phenolic pollutants (such as bisphenol A, phenol, 4-chlorophenol, etc.). Research results indicated that an efficient strategy for laccase immobilization to biodegrade phenolic pollutants was developed.


Assuntos
Poluentes Ambientais , Líquidos Iônicos , Lacase/química , Enzimas Imobilizadas/química , Polietilenoimina , Fenômenos Magnéticos
3.
Bioprocess Biosyst Eng ; 45(12): 1955-1966, 2022 Dec.
Artigo em Inglês | MEDLINE | ID: mdl-36355205

RESUMO

In this study, an amino-functionalized ionic liquid-modified magnetic chitosan (MACS-NIL) containing 2,2-diamine-di-3-ethylbenzothiazolin-6-sulfonic acid (ABTS) was used as a carrier, and dialdehyde starch (DAS) was used as a cross-linking agent to covalently immobilize laccase (MACS-NIL-DAS-lac), which realized the co-immobilization of laccase and ABTS. The carrier was characterized by Fourier infrared transform spectroscopy, scanning electron microscopy, thermogravimetric analysis, X-ray diffraction analysis, electron paramagnetic resonance, etc. The immobilization efficiency and activity retention of MACS-NIL-DAS-lac could reach 76.7% and 69.8%, respectively. At the same time, its pH stability, thermal stability, and storage stability had been significantly improved. In the organic pollutant removal performance test, the removal rate of 2,4-dichlorophenol (10 mg/L) by MACS-NIL-DAS-lac (1 U) could reach 100% within 6 h, and the removal efficiency could still reach 88.6% after six catalytic runs. In addition, MACS-NIL-DAS-lac also showed excellent degradation ability for other conventional phenolic pollutants and polycyclic aromatic hydrocarbons. The research results showed that MACS-NIL-DAS fabricated by the combination inorganic material, organic biomacromolecules, ionic liquid, and electron mediator could be used as a novel carrier for laccase immobilization and the immobilized laccase showed excellent removal efficiency for organic pollutants.


Assuntos
Quitosana , Poluentes Ambientais , Líquidos Iônicos , Nanoestruturas , Quitosana/química , Elétrons , Enzimas Imobilizadas/química , Lacase/química
4.
Front Bioeng Biotechnol ; 10: 946117, 2022.
Artigo em Inglês | MEDLINE | ID: mdl-35923578

RESUMO

Candida rugosa lipase (CRL) was activated with surfactants (sodium dodecyl sulfate [SDS]) and covalently immobilized onto a nanocomposite (Fe3O4-CS-DAC) fabricated by combining magnetic nanoparticles Fe3O4 with chitosan (CS) using polysaccharide macromolecule dialdehyde cellulose (DAC) as the cross-linking agent. Fourier transform infrared spectroscopy, transmission electron microscope, thermogravimetric analysis, and X-ray diffraction characterizations confirmed that the organic-inorganic nanocomposite support modified by DAC was successfully prepared. Enzymology experiments confirmed that high enzyme loading (60.9 mg/g) and 1.7 times specific enzyme activity could be obtained under the optimal immobilization conditions. The stability and reusability of immobilized CRL (Fe3O4-CS-DAC-SDS-CRL) were significantly improved simultaneously. Circular dichroism analysis revealed that the active conformation of immobilized CRL was maintained well. Results demonstrated that the inorganic-organic nanocomposite modified by carbohydrate polymer derivatives could be used as an ideal support for enzyme immobilization.

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