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
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