Magnetically Responsive PA6 Microparticles with Immobilized Laccase Show High Catalytic Efficiency in the Enzymatic Treatment of Catechol

Herewith we report the first attempt towards non-covalent immobilization of <i>Trametes versicolor</i> 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 suc...

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Bibliographic Details
Main Authors: Nadya Dencheva, Sandra Oliveira, Joana Braz, Dariya Getya, Marc Malfois, Zlatan Denchev, Ivan Gitsov
Format: Article
Language:English
Published: MDPI AG 2021-02-01
Series:Catalysts
Subjects:
Online Access:https://www.mdpi.com/2073-4344/11/2/239
Description
Summary:Herewith we report the first attempt towards non-covalent immobilization of <i>Trametes versicolor</i> 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 Fe<sub>3</sub>O<sub>4</sub> 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 determined. The reusability of the immobilized laccase-conjugates was proven for five consecutive oxidation cycles of catechol.
ISSN:2073-4344