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: Monteiro, Rodolpho R. C., Lima, Paula J. M., Pinheiro, Bruna B., Freire, Tiago M., Dutra, Lillian M. U., Fechine, Pierre B. A., Gonçalves, Luciana R. B., de Souza, Maria C. M., dos Santos, José C. S., Fernandez-Lafuente, Roberto
Format: Text
Language:English
Published: MDPI 2019
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Online Access:http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6720176/
http://www.ncbi.nlm.nih.gov/pubmed/31426510
https://doi.org/10.3390/ijms20164018
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spelling ftpubmed:oai:pubmedcentral.nih.gov:6720176 2023-05-15T13:52:34+02:00 Immobilization of Lipase A from Candida antarctica onto Chitosan-Coated Magnetic Nanoparticles Monteiro, Rodolpho R. C. Lima, Paula J. M. Pinheiro, Bruna B. Freire, Tiago M. Dutra, Lillian M. U. Fechine, Pierre B. A. Gonçalves, Luciana R. B. de Souza, Maria C. M. dos Santos, José C. S. Fernandez-Lafuente, Roberto 2019-08-17 http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6720176/ http://www.ncbi.nlm.nih.gov/pubmed/31426510 https://doi.org/10.3390/ijms20164018 en eng MDPI http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6720176/ http://www.ncbi.nlm.nih.gov/pubmed/31426510 http://dx.doi.org/10.3390/ijms20164018 © 2019 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/). CC-BY Article Text 2019 ftpubmed https://doi.org/10.3390/ijms20164018 2019-11-03T01:36:15Z 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 PubMed Central (PMC) International Journal of Molecular Sciences 20 16 4018
institution Open Polar
collection PubMed Central (PMC)
op_collection_id ftpubmed
language English
topic Article
spellingShingle Article
Monteiro, Rodolpho R. C.
Lima, Paula J. M.
Pinheiro, Bruna B.
Freire, Tiago M.
Dutra, Lillian M. U.
Fechine, Pierre B. A.
Gonçalves, Luciana R. B.
de Souza, Maria C. M.
dos Santos, José C. S.
Fernandez-Lafuente, Roberto
Immobilization of Lipase A from Candida antarctica onto Chitosan-Coated Magnetic Nanoparticles
topic_facet Article
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
author Monteiro, Rodolpho R. C.
Lima, Paula J. M.
Pinheiro, Bruna B.
Freire, Tiago M.
Dutra, Lillian M. U.
Fechine, Pierre B. A.
Gonçalves, Luciana R. B.
de Souza, Maria C. M.
dos Santos, José C. S.
Fernandez-Lafuente, Roberto
author_facet Monteiro, Rodolpho R. C.
Lima, Paula J. M.
Pinheiro, Bruna B.
Freire, Tiago M.
Dutra, Lillian M. U.
Fechine, Pierre B. A.
Gonçalves, Luciana R. B.
de Souza, Maria C. M.
dos Santos, José C. S.
Fernandez-Lafuente, Roberto
author_sort Monteiro, Rodolpho R. C.
title 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_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_sort immobilization of lipase a from candida antarctica onto chitosan-coated magnetic nanoparticles
publisher MDPI
publishDate 2019
url http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6720176/
http://www.ncbi.nlm.nih.gov/pubmed/31426510
https://doi.org/10.3390/ijms20164018
genre Antarc*
Antarctica
genre_facet Antarc*
Antarctica
op_relation http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6720176/
http://www.ncbi.nlm.nih.gov/pubmed/31426510
http://dx.doi.org/10.3390/ijms20164018
op_rights © 2019 by the authors.
Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
op_rightsnorm CC-BY
op_doi https://doi.org/10.3390/ijms20164018
container_title International Journal of Molecular Sciences
container_volume 20
container_issue 16
container_start_page 4018
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