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TitleMagnetically responsive PA6 microparticles with immobilized laccase show high catalytic efficiency in the enzymatic treatment of catechol
Author(s)Dencheva, Nadya Vasileva
Oliveira, Sandra Cristina Gomes
Braz, Joana Filipa Barros
Getya, Dariya
Malfois, Marc
Denchev, Z.
Gitsov, Ivan
Polyamide 6
Enzyme immobilization
Magnetic enzyme supports
Catechol oxidation
Issue date11-Feb-2021
PublisherMultidisciplinary Digital Publishing Institute (MDPI)
CitationDencheva, N.; Oliveira, S.; Braz, J.; Getya, D.; Malfois, M.; Denchev, Z.; Gitsov, I. Magnetically Responsive PA6 Microparticles with Immobilized Laccase Show High Catalytic Efficiency in the Enzymatic Treatment of Catechol. Catalysts 2021, 11, 239.
Abstract(s)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.
Publisher version
AccessOpen access
Appears in Collections:BUM - MDPI

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