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...

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Published in:International Journal of Molecular Sciences
Main Authors: 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
Format: Text
Language:English
Published: 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.
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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
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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