Commercial lipase from Burkholderia cepacia is immobilized on functionalized multi-walled carbon nanotubes (MWNT-COOH and MWNT-OH) provided by a physical adsorption. The immobilization processes for the carbon nanotubes are defined using immobilization time (0–30 min) and distinct...

Commercial lipase from Burkholderia cepacia is immobilized on functionalized multi-walled carbon nanotubes (MWNT-COOH and MWNT-OH) provided by a physical adsorption. The immobilization processes for the carbon nanotubes are defined using immobilization time (0–30 min) and distinct adsorbent:adsorbate ratios (1:4, 1:7, and 1:10) with lipase loading of 100, 175, and 250 mg, respectively. The characterization of the immobilized preparations, the free lipase, and the pure nanotubes (MWNT-COOH and MWNT-OH) indicate that the lipase adsorption is increased. Thermogravimetric analysis, differential scanning calorimetry, and scanning electron microscopy are used. The specific surface area, pore volumes, and average pore diameters are determined by nitrogen adsorption–desorption isotherms. For the pure lipase, in the range between 40 and 300 °C, the micrograph is acquired. Experimental results clearly show an effective lipase adsorption in a lower period of time (5 min) in MWNT-COOH and MWNT-OH as well as a decrease in the surface area (98.30–45.9(86) ± 2.5 and 97.61–37.71 ± 3.3(7) m2 g−1) and the pore volume (0.48–0.25 ± 0.01 and 0.39–0.24 ± 0.05 cm3 g−1), indicating that functionalized multi-walled carbon nanotubes can be successfully used as enzyme support

FUNDAÇÃO DE AMPARO À PESQUISA DO ESTADO DE SÃO PAULO - FAPESP

2012/05027-1

CONSELHO NACIONAL DE DESENVOLVIMENTO CIENTÍFICO E TECNOLÓGICO - CNPQ

310272/2017-3

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