Immobilization of lipase a from candida antarctica onto chitosan-coated magnetic nanoparticles
Autor: | Tiago M. Freire, Maria Cristiane Martins de Souza, Roberto Fernandez-Lafuente, Rodolpho R. C. Monteiro, Luciana Rocha Barros Gonçalves, Bruna B. Pinheiro, Pierre Basílio Almeida Fechine, Lillian Maria Uchôa Dutra, José C. S. dos Santos, Paula Jéssyca Morais Lima |
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Přispěvatelé: | 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) |
Rok vydání: | 2019 |
Předmět: |
magnetic nanoparticles
Immobilized enzyme Characterization 02 engineering and technology 01 natural sciences Article Catalysis Fungal Proteins Inorganic Chemistry Chitosan lcsh:Chemistry chemistry.chemical_compound Enzyme Stability characterization Physical and Theoretical Chemistry Lipase Fourier transform infrared spectroscopy Magnetite Nanoparticles Molecular Biology lcsh:QH301-705.5 Spectroscopy Candida biology 010405 organic chemistry fungi Organic Chemistry General Medicine Enzymes Immobilized equipment and supplies 021001 nanoscience & nanotechnology biology.organism_classification 0104 chemical sciences Computer Science Applications Thermogravimetry Lipase A from Candida antarctica chemistry lcsh:Biology (General) lcsh:QD1-999 Covalent bond Magnetic nanoparticles biology.protein lipase A from Candida antarctica Candida antarctica Glutaraldehyde chitosan 0210 nano-technology Nuclear chemistry |
Zdroj: | Digital.CSIC. Repositorio Institucional del CSIC instname International Journal of Molecular Sciences, Vol 20, Iss 16, p 4018 (2019) International Journal of Molecular Sciences Volume 20 Issue 16 |
Popis: | 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&ndash 11 times higher than that of the soluble enzyme at pH 5&ndash 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. |
Databáze: | OpenAIRE |
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