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Study of the interaction of the lactase enzyme immobilized in a carbon nanotube matrix for the development of the chemically modified carbon paste electrode

2020; Elsevier BV; Volume: 20; Linguagem: Inglês

10.1016/j.surfin.2020.100592

2468-0230

Aila Riany de Brito, Iasnaia Maria de Carvalho Tavares, Marise Silva de Carvalho, Adriana Jesus de Oliveira, Luiz Carlos Salay, Antônio de Santana Santos, Paulo Neilson Marques dos Anjos, Julieta Rangel de Oliveira, Marcelo Franco,

Photoreceptor and optogenetics research

The innovative aspect of nanoparticles takes on an important role in the advancement of research on nanostructured materials. The objective of the present study was to carry out an investigation of the interactions between lactase enzyme and carbon nanotubes applied to the elaboration of a chemically modified carbon paste electrode. Scanning electron microscopy (SEM), transmission electron microscopy (TEM), fluorescence spectroscopy, Fourier-transform infrared spectroscopy (FTIR), X-ray diffraction (XRD), and thermogravimetric (TG/DTG) were conducted to comprehend the interactions and the efficiency of the enzyme immobilization in carbon nanotubes. Through studying the morphology of the materials using SEM and TEM, it was shown that there was adsorption of the lactase enzyme into the tubular area of the carbon nanotubes. Through fluorescence spectroscopy analysis, it was observed that the emission of lactase fluorescence is mainly due to tryptophan residue (Trp), and this fluorescence was reduced in the presence of CNT, demonstrating the interaction between these components. In the remaining analyses, FTIR, XRD and TG/DTG, adsorption of the lactase enzyme into the carbon nanotube matrix was demonstrated.