Immobilization of Lipase A from Candida antarctica onto Chitosan-Coated Magnetic Nanoparticles
In this communication, lipase A from Candida antarctica (CALA) was immobilized by covalent bonding on magnetic nanoparticles coated with chitosan and activated with glutaraldehyde, labelled CALA-MNP, (immobilization parameters: 84.1% ± 1.0 for immobilization yield and 208.0 ± 3.0 U/g ± 1.1 for deriv...
Published in: | International Journal of Molecular Sciences |
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Main Authors: | , , , , , , , , , |
Format: | Text |
Language: | English |
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Multidisciplinary Digital Publishing Institute
2019
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Online Access: | https://doi.org/10.3390/ijms20164018 |
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author | Rodolpho R. C. Monteiro Paula J. M. Lima Bruna B. Pinheiro Tiago M. Freire Lillian M. U. Dutra Pierre B. A. Fechine Luciana R. B. Gonçalves Maria C. M. de Souza José C. S. dos Santos Roberto Fernandez-Lafuente |
author_facet | Rodolpho R. C. Monteiro Paula J. M. Lima Bruna B. Pinheiro Tiago M. Freire Lillian M. U. Dutra Pierre B. A. Fechine Luciana R. B. Gonçalves Maria C. M. de Souza José C. S. dos Santos Roberto Fernandez-Lafuente |
author_sort | Rodolpho R. C. Monteiro |
collection | MDPI Open Access Publishing |
container_issue | 16 |
container_start_page | 4018 |
container_title | International Journal of Molecular Sciences |
container_volume | 20 |
description | In this communication, lipase A from Candida antarctica (CALA) was immobilized by covalent bonding on magnetic nanoparticles coated with chitosan and activated with glutaraldehyde, labelled CALA-MNP, (immobilization parameters: 84.1% ± 1.0 for immobilization yield and 208.0 ± 3.0 U/g ± 1.1 for derivative activity). CALA-MNP biocatalyst was characterized by X-ray Powder Diffraction (XRPD), Fourier Transform Infrared (FTIR) spectroscopy, Thermogravimetry (TG) and Scanning Electron Microscope (SEM), proving the incorporation of magnetite and the immobilization of CALA in the chitosan matrix. Besides, the immobilized biocatalyst showed a half-life 8–11 times higher than that of the soluble enzyme at pH 5–9. CALA showed the highest activity at pH 7, while CALA-MNP presented the highest activity at pH 10. The immobilized enzyme was more active than the free enzyme at all studied pH values, except pH 7. |
format | Text |
genre | Antarc* Antarctica |
genre_facet | Antarc* Antarctica |
id | ftmdpi:oai:mdpi.com:/1422-0067/20/16/4018/ |
institution | Open Polar |
language | English |
op_collection_id | ftmdpi |
op_coverage | agris |
op_doi | https://doi.org/10.3390/ijms20164018 |
op_relation | Materials Science https://dx.doi.org/10.3390/ijms20164018 |
op_rights | https://creativecommons.org/licenses/by/4.0/ |
op_source | International Journal of Molecular Sciences; Volume 20; Issue 16; Pages: 4018 |
publishDate | 2019 |
publisher | Multidisciplinary Digital Publishing Institute |
record_format | openpolar |
spelling | ftmdpi:oai:mdpi.com:/1422-0067/20/16/4018/ 2025-01-16T19:39:17+00:00 Immobilization of Lipase A from Candida antarctica onto Chitosan-Coated Magnetic Nanoparticles Rodolpho R. C. Monteiro Paula J. M. Lima Bruna B. Pinheiro Tiago M. Freire Lillian M. U. Dutra Pierre B. A. Fechine Luciana R. B. Gonçalves Maria C. M. de Souza José C. S. dos Santos Roberto Fernandez-Lafuente agris 2019-08-17 application/pdf https://doi.org/10.3390/ijms20164018 EN eng Multidisciplinary Digital Publishing Institute Materials Science https://dx.doi.org/10.3390/ijms20164018 https://creativecommons.org/licenses/by/4.0/ International Journal of Molecular Sciences; Volume 20; Issue 16; Pages: 4018 lipase A from Candida antarctica chitosan magnetic nanoparticles characterization Text 2019 ftmdpi https://doi.org/10.3390/ijms20164018 2023-07-31T22:31:45Z In this communication, lipase A from Candida antarctica (CALA) was immobilized by covalent bonding on magnetic nanoparticles coated with chitosan and activated with glutaraldehyde, labelled CALA-MNP, (immobilization parameters: 84.1% ± 1.0 for immobilization yield and 208.0 ± 3.0 U/g ± 1.1 for derivative activity). CALA-MNP biocatalyst was characterized by X-ray Powder Diffraction (XRPD), Fourier Transform Infrared (FTIR) spectroscopy, Thermogravimetry (TG) and Scanning Electron Microscope (SEM), proving the incorporation of magnetite and the immobilization of CALA in the chitosan matrix. Besides, the immobilized biocatalyst showed a half-life 8–11 times higher than that of the soluble enzyme at pH 5–9. CALA showed the highest activity at pH 7, while CALA-MNP presented the highest activity at pH 10. The immobilized enzyme was more active than the free enzyme at all studied pH values, except pH 7. Text Antarc* Antarctica MDPI Open Access Publishing International Journal of Molecular Sciences 20 16 4018 |
spellingShingle | lipase A from Candida antarctica chitosan magnetic nanoparticles characterization Rodolpho R. C. Monteiro Paula J. M. Lima Bruna B. Pinheiro Tiago M. Freire Lillian M. U. Dutra Pierre B. A. Fechine Luciana R. B. Gonçalves Maria C. M. de Souza José C. S. dos Santos Roberto Fernandez-Lafuente Immobilization of Lipase A from Candida antarctica onto Chitosan-Coated Magnetic Nanoparticles |
title | Immobilization of Lipase A from Candida antarctica onto Chitosan-Coated Magnetic Nanoparticles |
title_full | Immobilization of Lipase A from Candida antarctica onto Chitosan-Coated Magnetic Nanoparticles |
title_fullStr | Immobilization of Lipase A from Candida antarctica onto Chitosan-Coated Magnetic Nanoparticles |
title_full_unstemmed | Immobilization of Lipase A from Candida antarctica onto Chitosan-Coated Magnetic Nanoparticles |
title_short | Immobilization of Lipase A from Candida antarctica onto Chitosan-Coated Magnetic Nanoparticles |
title_sort | immobilization of lipase a from candida antarctica onto chitosan-coated magnetic nanoparticles |
topic | lipase A from Candida antarctica chitosan magnetic nanoparticles characterization |
topic_facet | lipase A from Candida antarctica chitosan magnetic nanoparticles characterization |
url | https://doi.org/10.3390/ijms20164018 |