Seleção de suportes para imobilização de lipases
In this work, lipases (lip) from Burkholderia lataLBBIO-BL02 were immobilized on different supports, by physical adsorption and applied in ester hydrolysis reactions. The supports studied were: (1) Cobalt magnetic oxide (OMC); (2) expandedmesoporous silica (SMP); (3) metal–organic frameworks of Fe...
| Autor principal: | RODRIGUES, RICARDO DE SOUSA |
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| Formato: | Trabalho de Conclusão de Curso (Graduação) |
| Idioma: | Português |
| Publicado em: |
Universidade Tecnológica Federal do Paraná
2021
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| Assuntos: | |
| Acesso em linha: |
http://repositorio.utfpr.edu.br/jspui/handle/1/25566 |
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| Resumo: |
In this work, lipases (lip) from Burkholderia lataLBBIO-BL02 were immobilized on different supports, by physical adsorption and applied in ester hydrolysis reactions. The supports studied were: (1) Cobalt magnetic oxide (OMC); (2) expandedmesoporous silica (SMP); (3) metal–organic frameworks of Fe (III) ion (MOF) and (4) polymer produced by electrospinning based on chitosan (QE). Immobilization efficiency (E) and activity retention (R) were measured by hydrolysis of p-nitrophenyl palmitate (pNPP). The immobilization efficiency (E) was 68%, 73 and 90% respectively for the OMC. There was not enzymatic immobilization for the QE. Activity (R) retention was 170% for SMP-lip and 400% for MOF-lip. There was no retention of activity for the OMC. The enzyme immobilized on the best support (highest E and R) was studied for stability in organic solvents (1 h; 25 °C): methanol (log P -0.76), isopropanol (log P -0.28), ethanol (log P -0.24), acetone (log P -0.23), n-hexane (log P -3.50) and n-heptane (log P -4.0). The residual activities were carried by hydrolysis of the pNPP. Results showed that MOF-lip lost 60 and 30% of the catalytic activity when incubated in methanol and n-heptane, respectively. For other solvents, activity retention was 100%. Hydrolysis reactions of vegetable oils (olive, corn and sunflower) were carried out with MOF-lip. The activity was 3200 U mg-1for the hydrolysis of olive oil and 2800 U mg-1for corn and sunflower oils. The results indicated that MOF is a promising support for immobilizing lipases and for use in ester hydrolysis reactions. |
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