Biotransformação empregando lipases ligadas ao micélio
Lipases of Botryosphaeria ribis EC-01 bound to the mycelium, from submerged fermentation, were used as catalysts in biocatalysis. Were studied : a) Stability at temperature (40, 50 and 55 ° C, 3 h) through the hydrolysis reaction of p-nitrophenyl palmitate (pNPP); b) Synthesis of ethyl oleate (Lowry...
| Autor principal: | Igarashi, Gabriella Sadako |
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| Formato: | Trabalho de Conclusão de Curso (Graduação) |
| Idioma: | Português |
| Publicado em: |
Universidade Tecnológica Federal do Paraná
2020
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| Assuntos: | |
| Acesso em linha: |
http://repositorio.utfpr.edu.br/jspui/handle/1/5494 |
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| Resumo: |
Lipases of Botryosphaeria ribis EC-01 bound to the mycelium, from submerged fermentation, were used as catalysts in biocatalysis. Were studied : a) Stability at temperature (40, 50 and 55 ° C, 3 h) through the hydrolysis reaction of p-nitrophenyl palmitate (pNPP); b) Synthesis of ethyl oleate (Lowry-Tinsley method), with and without cosolvent (hexane). For the latter case, an experimental design 23 (Ttemperature, mass of mycelium-MM and acid molar ratio: alcohol-MR) with triplicate at the central point was performed. The initial mycelial activity was calculated prior to the thermal stability study (2.71 ± 0.27 U mg-1). The study of the thermal stability of the mycelium demonstrated enzymatic loss of approximately 20% for all temperatures studied. The influence of the co-solvent (hexane) on the yield of the ethyl oleate synthesis by the mycelium was positive with best results 90 (40°C; 1 g of mycelium and MR 1:1) and 97% (40°; 1 g of mycelium and MR 1:3) yield for the times of 24 and 48h respectively. Analyzing the amount of electric energy, maintenance of the catalytic activity of the enzyme and calculation of the productivity in the ester (36 μmol h-1 g-1 / 24 h 20 μmol h-1 g-1), the reaction for 24 h was more viable. Thus, lipases of Botryosphaeria ribis EC-01 bound to the mycelium may be an interesting alternative to immobilized lipases, in the synthesis of ethyl oleate and other esters, due to their preparation of low cost and high enzymatic activity. |
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