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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Bibliographic Details
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., Santos, José C. S. dos, Fernández-Lafuente, Roberto
Other Authors: Fundação Cearense de Apoio ao Desenvolvimento Científico e Tecnológico, Conselho Nacional de Desenvolvimento Científico e Tecnológico (Brasil), Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (Brasil), Ministerio de Economía y Competitividad (España)
Format: Article in Journal/Newspaper
Language:English
Published: Multidisciplinary Digital Publishing Institute 2019
Subjects:
Lipase A from Candida antarctica
Chitosan
Magnetic nanoparticles
Characterization
Antarc*
Antarctica
Online Access:http://hdl.handle.net/10261/188976
https://doi.org/10.3390/ijms20164018
https://doi.org/10.13039/501100003593
https://doi.org/10.13039/501100002322
https://doi.org/10.13039/501100005283
https://doi.org/10.13039/501100003329
Description
Summary: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. This research was funded by Fundação Cearense de Apoio ao Desenvolvimento Científico e Tecnológico (FUNCAP), grant numbers BP3-0139-00005.01.00/18 and PNE-0112-00048.01.00/16, Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq), grant numbers 422942/2016-2, 409058/2015-5 and 408790/2016-4, Coordenação de Aperfeiçoamento de Ensino Superior (CAPES-Finance Code 001) and MICIU, grant number CTQ2015-68951-C3-3-R. Peer reviewed

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