Fixation of laccase enzyme into polypyrrole, assisted by chemical interaction with modified magnetite nanoparticles: A facile route to synthesize stable electroactive bionanocomposite catalysts (original) (raw)
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Ferromagnetic nanoparticles synthesis and functionalization for laccase enzyme immobilization
Materials Today: Proceedings, 2022
Ferromagnetic nanomaterials can easily be separated from the reaction media by using external magnetic force. Nanoparticles are excellent supporting materials that provide large surface area with high mass transfer rate. Ferromagnetic nanoparticle considered as an ideal immobilization supporting materials of biocatalysts for easy and fast recovery. In this study, ferromagnetic iron oxide nanoparticles were synthesized and functionalized as immobilization support materials. Amino functionalization of nanoparticles was performed to improve thermal stability and enzymatic activity. XRD planes at 2h confirmed the successful synthesis of ferromagnetic nanoparticles. FTIR spectrum used to identify amino functionalization of nanoparticles, and size and surface morphology were studied through transmission electron microscopy (TEM).
Applied Sciences, 2017
Oxidative biocatalysis by laccase arises as a promising alternative in the development of advanced oxidation processes for the removal of xenobiotics. The aim of this work is to develop various types of nanobiocatalysts based on laccase immobilized on different superparamagnetic and non-magnetic nanoparticles to improve the stability of the biocatalysts. Several techniques of enzyme immobilization were evaluated based on ionic exchange and covalent bonding. The highest yields of laccase immobilization were achieved for the covalent laccase nanoconjugates of silica-coated magnetic nanoparticles (2.66 U mg−1 NPs), formed by the covalent attachment of the enzyme between the aldehyde groups of the glutaraldehyde-functionalized nanoparticle and the amino groups of the enzyme. Moreover, its application in the biotransformation of phenol as a model recalcitrant compound was tested at different pH and successfully achieved at pH 6 for 24 h. A sequential batch operation was carried out, with...
International journal of biological macromolecules, 2018
Magnetite and magnetite core/shell (FeO/SiO) nanoparticles were synthesized and functionalized with two different alkyl chain length linkers that were 3-Phosphonopropionic acid (3-PPA) and 16-Phosphonohexadecanoic acid (16-PHDA). Xylanase (EC 3.2.1.8, endo-1,4-xylanase, endo-1), was immobilized on as synthesized bare and silica coated magnetite nanoparticles via well-known EDC coupling. Transmission Electron Microscopy (TEM), Field Emission Scanning Electron Microscopy (FESEM), X-Ray Diffraction Spectroscopy (XRD), X-ray Photoelectron Spectroscopy (XPS), Dynamic Light Scattering (DLS) and Thermogravimetric analysis (TGA) techniques were utilized to characterize all the modifications. The flexible linker chain length plays a vital role in the catalytic attributes of the immobilized enzyme. Result shows that long chain alkyl linker grafted magnetite and magnetite core/silica shell nanoparticles exhibited a superior performance in terms of lower K, higher catalytic efficiency and bette...
Catalysts
Herewith we report the first attempt towards non-covalent immobilization of Trametes versicolor laccase on neat and magnetically responsive highly porous polyamide 6 (PA6) microparticles and their application for catechol oxidation. Four polyamide supports, namely neat PA6 and such carrying Fe, phosphate-coated Fe and Fe3O4 cores were synthesized in suspension by activated anionic ring-opening polymerization (AAROP) of ε-caprolactam (ECL). Enzyme adsorption efficiency up to 92% was achieved in the immobilization process. All empty supports and PA6 laccase complexes were characterized by spectral and synchrotron WAXS/SAXS analyses. The activity of the immobilized laccase was evaluated using 2,2’-Azino-bis-(3- ethylbenzothiazoline-6-sulfonic acid (ABTS) and compared to the native enzyme. The PA6 laccase conjugates displayed up to 105% relative activity at room temperature, pH 4, 40 °C and 20 mM ionic strength (citrate buffer). The kinetic parameters of the ABTS oxidation were also det...
Synthesis and characterization of functionalized nanoparticles for lactase immobilization (Atena Editora), 2022
This work focused on the development and characterization of nanoparticles, a branch that is constantly growing and through recent research it has been shown that, no matter how small a particle, it can drive great technological advances. Nanoparticles that have a high surface area cover biotechnological, chemical, physical and even electronic areas due to the great versatility present in their structures. Its functionalization is necessary in order to set desirable properties. As practical objectives, magnetic nanoparticles were synthesized from iron (II) and (III) chlorides and sodium hydroxide and later functionalized with APTS and, submitting the samples to analyzes such as X-Ray Diffractions (XRD), Infrared Spectroscopy ( FTIR) and Zeta Potential, in order to confirm the synthesis and functionalization.
Development of a Four-Enzyme Magnetic Nanobiocatalyst for Multi-Step Cascade Reactions
Catalysts
We report the preparation, characterization and application of a novel magnetic four-enzyme nanobiocatalyst prepared by the simultaneous covalent co-immobilization of cellulase (CelDZ1), β-glucosidase (bgl), glucose oxidase (GOx) and horseradish peroxidase (HRP) onto the surface of amino-functionalized magnetic nanoparticles (MNPs). This nanobiocatalyst was characterized by various spectroscopic techniques. The co-immobilization process yielded maximum recovered enzymatic activity (CelDZ1: 42%, bgl: 66%, GOx: 94% and HRP: 78%) at a 10% v/v cross-linker concentration, after 2 h incubation time and at 1:1 mass ratio of MNPs to total enzyme content. The immobilization process leads to an increase of Km and a decrease of Vmax values of co-immobilized enzymes. The thermal stability studies of the co-immobilized enzymes indicated up to 2-fold increase in half-life time constants and up to 1.5-fold increase in their deactivation energies compared to the native enzymes. The enhanced thermod...