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DC Field | Value | Language |
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dc.contributor.author | Oliveira, Raysa Ramos de | |
dc.date.accessioned | 2023-12-22T02:45:38Z | - |
dc.date.available | 2023-12-22T02:45:38Z | - |
dc.date.issued | 2019-08-14 | |
dc.identifier.citation | OLIVEIRA, Raysa Ramos de. Efeito do CO2 em condições supercríticas como pré-tratamento da lipase de Thermomyces lanuginosus imobilizada. 2019. 169 f. Dissertação (Mestrado em Engenharia Química) - Instituto de Tecnologia, Departamento de Engenharia Química, Universidade Federal Rural do Rio de Janeiro, Seropédica, 2019. | por |
dc.identifier.uri | https://rima.ufrrj.br/jspui/handle/20.500.14407/13332 | - |
dc.description.abstract | As enzimas apresentam uma grande perspectiva considerando sua aplicação como biocatalisador nos mais diversos segmentos. Contudo, seu elevado custo e baixa estabilidade são ainda considerados fatores limitantes em processos de escala industrial. Por esse motivo, estudos focados na imobilização e, recentemente, no pré-tratamento utilizando meios não convencionais têm se mostrado favoráveis frente à essas desvantagens. A presente dissertação teve como objetivo imobilizar a lipase de Thermomyces lanuginosus (TLL) em suportes aniônico (Amberlite IRA400 Cl-) e catiônico (Amberlite IR120 Na+) por meio da adsorção iônica, em seguida, avaliar os efeitos da condição supercrítica do CO2 sobre a TLL imobilizada e compará-la com a TLL comecial (Lipozyme TL IM). Foi observado que o suporte Amberlite IRA400 Cl- apresentou melhores resultados de atividade e teor de proteína frente ao Amberlite IR120 Na+. Posteriormente, os efeitos das condições supercríticas do dióxido de carbono sobre a atividade hidrolítica e estabilidade enzimática também foram avaliados. Os experimentos foram conduzidos de acordo com um planejamento experimental, variando a temperatura de 35 a 75 ºC, a pressão de 80 a 300 bar e o tempo de exposição de 1 a 6 h. Os resultados mostraram uma redução da atividade da TLL imobilizada em Amberlite IR120 Na+ em todas as condições propostas. Por outro lado, foi observado uma superativação em até 57% em relação a atividade medida antes do pré-tratamento para a TLL imobilizada em Amberlite IRA400 Cl-. Em seguida, o mesmo procedimento experimental foi aplicado à Lipozyme TL IM. Para este, foi notado uma superativação de 18% na mesma condição proposta para a TLL imobilizada em Amberlite IRA400 Cl- (75 ºC, 300 bar e 6 h). Em relação às mudanças nas ligações presentes no suporte e na enzima, não foram observadas alterações relevantes. Contudo, foi possível observar pela análise de calorimetria exploratória diferencial que o CO2 atuou com um protetor no complexo enzima-suporte para a Lipozyme TL IM aumentando a estabilidade dessa lipase, enquanto que nos outros suportes foi observado uma maior degradação das proteínas. Por último, foi verificado que o aumento da concentração do substrato (p-nitrofenil laurato) acarretou em uma inativação tanto da lipase livre, quanto na imobilizada em Amberlite IRA400 Cl- e comercialmente. Sendo o maior efeito observado na TLL imobilizada em Amberlite IRA400 CI- | por |
dc.description.sponsorship | CAPES - Coordenação de Aperfeiçoamento de Pessoal de Nível Superior | por |
dc.description.sponsorship | CNPq - Conselho Nacional de Desenvolvimento Científico e Tecnológico | por |
dc.description.sponsorship | FAPERJ - Fundação Carlos Chagas Filho de Amparo à Pesquisa do Estado do Rio de Janeiro | por |
dc.format | application/pdf | * |
dc.language | por | por |
dc.publisher | Universidade Federal Rural do Rio de Janeiro | por |
dc.rights | Acesso Aberto | por |
dc.subject | Lipases | por |
dc.subject | Imobilização de enzimas | por |
dc.subject | Fluido supercrítico | por |
dc.subject | Planejamento experimental | por |
dc.subject | Enzyme immobilization | eng |
dc.subject | Supercritical fluid | eng |
dc.subject | Experimental design | eng |
dc.title | Efeito do CO2 em condições supercríticas como pré-tratamento da lipase de Thermomyces lanuginosus imobilizada | por |
dc.type | Dissertação | por |
dc.description.abstractOther | Enzymes present a great perspective considering their application as a biocatalyst in the many sectors. However, their high cost and low stability are still considered limiting factors in industrial-scale processes. For this reason, studies focused on immobilization and, recently, pretreatment using non-conventional media have been favorable in view of these disadvantages. This dissertation aimed to immobilize Thermomyces lanuginosus lipase (TLL) in anionic (Amberlite IRA400 Cl-) and cationic (Amberlite IR120 Na+) supports by ionic adsorption, then evaluate the effects of the supercritical condition of CO2 on Immobilized TLL and compare it with the commercial TLL (Lipozyme TL IM). It was observed that the support Amberlite IRA400 Cl- presented better results of activity and protein content compared to Amberlite IR120 Na+. Afterward, the effects of carbon dioxide supercritical conditions on hydrolytic activity and enzymatic stability were evaluated. The experiments were conducted according to experimental design, varying the temperature from 35 to 75 ºC, the pressure from 80 to 300 bar and the exposure time from 1 to 6 h. The results showed an inactivation of immobilized TLL in Amberlite IR120 Na+ under all proposed conditions. On the other hand, it was observed an overactivation up to 57% in relation to of activity measured before pretreatment for immobilized TLL in Amberlite IRA400 Cl-. Then, the same experimental procedure was applied to Lipozyme TL IM (commercially immobilized lipase), aiming at a comparison between commercial and immobilized lipase in this study. For this, an overactivation of 18% was noted under the same condition proposed for TLL immobilized on Amberlite IRA400 Cl- (75 ºC, 300 bar, and 6 h). Regarding changes in the chemical binding of support and enzyme, no relevant changes were observed. However, it was possible to observe that by the differential exploratory calorimetry analysis that CO2 acted as a protector for Lipozyme TL IM increasing the stability of this lipase, while in the other supports a greater protein degradation was observed. Finally, it was found that the increase in substrate concentration (p-nitrophenyl laurate) resulted in inactivation of both free and immobilized lipase in Amberlite IRA400 Cl- and commercially. Being the largest effect observed on the immobilized TLL in Amberlite IRA400 Cl-. | eng |
dc.contributor.advisor1 | Brígida, Ana Iraidy Santa | |
dc.contributor.advisor1ID | 847.843.343-00 | por |
dc.contributor.advisor-co1 | Mendes, Marisa Fernandes | |
dc.contributor.advisor-co1ID | 023.918.187-50 | por |
dc.contributor.referee1 | Brígida, Ana Iraidy Santa | |
dc.contributor.referee2 | Mendes, Marisa Fernandes | |
dc.contributor.referee3 | Pereira, Cristiane de Souza Siqueira | |
dc.contributor.referee4 | Gottschalk, Leda Maria Fortes | |
dc.contributor.referee5 | Oliveira, Renata Nunes | |
dc.creator.ID | 145.327.977-64 | por |
dc.creator.Lattes | http://lattes.cnpq.br/4636322945072582 | por |
dc.publisher.country | Brasil | por |
dc.publisher.department | Instituto de Tecnologia | por |
dc.publisher.initials | UFRRJ | por |
dc.publisher.program | Programa de Pós-Graduação em Engenharia Química | por |
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