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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| Format: | Article |
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MDPI AG
2021-02-01
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| Series: | Catalysts |
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| Online Access: | https://www.mdpi.com/2073-4344/11/2/239 |
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| author | Nadya Dencheva Sandra Oliveira Joana Braz Dariya Getya Marc Malfois Zlatan Denchev Ivan Gitsov |
| author_facet | Nadya Dencheva Sandra Oliveira Joana Braz Dariya Getya Marc Malfois Zlatan Denchev Ivan Gitsov |
| author_sort | Nadya Dencheva |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-03-09T04:43:00Z |
| format | Article |
| id | doaj.art-6ff2e130c63b4be6857f9e3cd11d9a36 |
| institution | Directory Open Access Journal |
| issn | 2073-4344 |
| language | English |
| last_indexed | 2024-03-09T04:43:00Z |
| publishDate | 2021-02-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Catalysts |
| spelling | doaj.art-6ff2e130c63b4be6857f9e3cd11d9a362023-12-03T13:18:31ZengMDPI AGCatalysts2073-43442021-02-0111223910.3390/catal11020239Magnetically Responsive PA6 Microparticles with Immobilized Laccase Show High Catalytic Efficiency in the Enzymatic Treatment of CatecholNadya Dencheva0Sandra Oliveira1Joana Braz2Dariya Getya3Marc Malfois4Zlatan Denchev5Ivan Gitsov6IPC-Institute for Polymers and Composites, University of Minho, 4800-056 Guimaraes, PortugalIPC-Institute for Polymers and Composites, University of Minho, 4800-056 Guimaraes, PortugalIPC-Institute for Polymers and Composites, University of Minho, 4800-056 Guimaraes, PortugalDepartment of Chemistry, State University of New York, Syracuse, NY 13210, USAALBA Synchrotron Facility, Cerdanyola del Valés, 0890 Barcelona, SpainIPC-Institute for Polymers and Composites, University of Minho, 4800-056 Guimaraes, PortugalDepartment of Chemistry, State University of New York, Syracuse, NY 13210, USAHerewith 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.https://www.mdpi.com/2073-4344/11/2/239laccasepolyamide 6enzyme immobilizationmagnetic enzyme supportscatechol oxidation |
| spellingShingle | Nadya Dencheva Sandra Oliveira Joana Braz Dariya Getya Marc Malfois Zlatan Denchev Ivan Gitsov Magnetically Responsive PA6 Microparticles with Immobilized Laccase Show High Catalytic Efficiency in the Enzymatic Treatment of Catechol Catalysts laccase polyamide 6 enzyme immobilization magnetic enzyme supports catechol oxidation |
| title | Magnetically Responsive PA6 Microparticles with Immobilized Laccase Show High Catalytic Efficiency in the Enzymatic Treatment of Catechol |
| title_full | Magnetically Responsive PA6 Microparticles with Immobilized Laccase Show High Catalytic Efficiency in the Enzymatic Treatment of Catechol |
| title_fullStr | Magnetically Responsive PA6 Microparticles with Immobilized Laccase Show High Catalytic Efficiency in the Enzymatic Treatment of Catechol |
| title_full_unstemmed | Magnetically Responsive PA6 Microparticles with Immobilized Laccase Show High Catalytic Efficiency in the Enzymatic Treatment of Catechol |
| title_short | Magnetically Responsive PA6 Microparticles with Immobilized Laccase Show High Catalytic Efficiency in the Enzymatic Treatment of Catechol |
| title_sort | magnetically responsive pa6 microparticles with immobilized laccase show high catalytic efficiency in the enzymatic treatment of catechol |
| topic | laccase polyamide 6 enzyme immobilization magnetic enzyme supports catechol oxidation |
| url | https://www.mdpi.com/2073-4344/11/2/239 |
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