Modelagem fenomenológica da síntese enzimática de biodiesel etanólico utilizando lipase solúvel

Detalhes bibliográficos
Autor(a) principal: Villegas Aguilar, María Carlota
Data de Publicação: 2018
Tipo de documento: Dissertação
Idioma: por
Título da fonte: Repositório Institucional da UFSCAR
Texto Completo: https://repositorio.ufscar.br/handle/ufscar/11804
Resumo: The kinetics study of the synthesis of ethyl biodiesel allows a deeper understanding of the enzymatic process, providing an important tool for process design, optimization and control. Most of the models proposed in the literature for enzymatic biodiesel production use methanol and immobilized lipases. Moreover, depending on the source of the lipase and the reaction medium, the reaction may have a distinct mechanism. In this work we study the biodiesel production by transesterification of refined soybean oil and bioethanol using the soluble lipase NS-40116, a liquid formulation of a genetic modified lipase from Thermomyces lanuginosus. The aim of this research is to develop a phenomenological model capable of describing the catalytic behavior of that lipase formulation in this heterogeneous medium. Batch assays were carried out in a bench jacketed glass reactor where several process variables were varied: agitation speed (800-1200 rpm), enzyme concentration (0.5-2.0%w/woil) and alcohol content (1.5-2.0 equivalent). All assays were carried out at 35°C with 10%w/woil of water. In addition, the relationship between the agitation speed and the volumetric flow rate of the substrates with the oil-water-alcohol emulsion interface was determined. The soluble lipase NS-40116 was characterized: protein content 31.454 ± 0.002 mg protein/ml lipase, hydrolytic activity 48048 ± 653 LU/ml (1 LU: activity required to produce 1 μmol/min with standard conditions) and molecular weight 31 kDa. An ethyl biodiesel was obtained from refined soybean oil with a concentration of esters: 82.55 ± 7.17% (T = 35°C, 800 RPM, 10%w/woil water, 2.0%w/woil lipase and 2.0 eq. ethyl alcohol). The average interfacial area was evaluated by measuring droplet diameters distribution in pictures of the emulsion obtained in a microscope. Different agitation speeds and polar/nonpolar volume ratios were used. Results show that the average diameter of the droplets increases when the polar volume increases and decreases with the agitation speed. The kinetic parameters were determined for the mathematical model of the enzymatic synthesis of ethyl biodiesel using the soluble lipase NS-40116.
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spelling Villegas Aguilar, María CarlotaRibeiro, Marcelo Perencin de Arrudahttp://lattes.cnpq.br/0381402687491195Giordano, Roberto de Camposhttp://lattes.cnpq.br/0834668419587001http://lattes.cnpq.br/3753884975348864e44c2c4d-42d1-42b7-b963-afd00d53f7822019-09-09T17:07:41Z2019-09-09T17:07:41Z2018-03-27VILLEGAS AGUILAR, María Carlota. Modelagem fenomenológica da síntese enzimática de biodiesel etanólico utilizando lipase solúvel. 2018. Dissertação (Mestrado em Engenharia Química) – Universidade Federal de São Carlos, São Carlos, 2018. Disponível em: https://repositorio.ufscar.br/handle/ufscar/11804.https://repositorio.ufscar.br/handle/ufscar/11804The kinetics study of the synthesis of ethyl biodiesel allows a deeper understanding of the enzymatic process, providing an important tool for process design, optimization and control. Most of the models proposed in the literature for enzymatic biodiesel production use methanol and immobilized lipases. Moreover, depending on the source of the lipase and the reaction medium, the reaction may have a distinct mechanism. In this work we study the biodiesel production by transesterification of refined soybean oil and bioethanol using the soluble lipase NS-40116, a liquid formulation of a genetic modified lipase from Thermomyces lanuginosus. The aim of this research is to develop a phenomenological model capable of describing the catalytic behavior of that lipase formulation in this heterogeneous medium. Batch assays were carried out in a bench jacketed glass reactor where several process variables were varied: agitation speed (800-1200 rpm), enzyme concentration (0.5-2.0%w/woil) and alcohol content (1.5-2.0 equivalent). All assays were carried out at 35°C with 10%w/woil of water. In addition, the relationship between the agitation speed and the volumetric flow rate of the substrates with the oil-water-alcohol emulsion interface was determined. The soluble lipase NS-40116 was characterized: protein content 31.454 ± 0.002 mg protein/ml lipase, hydrolytic activity 48048 ± 653 LU/ml (1 LU: activity required to produce 1 μmol/min with standard conditions) and molecular weight 31 kDa. An ethyl biodiesel was obtained from refined soybean oil with a concentration of esters: 82.55 ± 7.17% (T = 35°C, 800 RPM, 10%w/woil water, 2.0%w/woil lipase and 2.0 eq. ethyl alcohol). The average interfacial area was evaluated by measuring droplet diameters distribution in pictures of the emulsion obtained in a microscope. Different agitation speeds and polar/nonpolar volume ratios were used. Results show that the average diameter of the droplets increases when the polar volume increases and decreases with the agitation speed. The kinetic parameters were determined for the mathematical model of the enzymatic synthesis of ethyl biodiesel using the soluble lipase NS-40116.O estudo da cinética da síntese de biodiesel permite uma melhor compreensão de seu processo da produção. Os modelos cinéticos que têm sido sugeridos para a produção do biodiesel por catálise enzimática são diversos, sendo a maior parte para lipases imobilizadas. Cada lipase tem um mecanismo de reação distinto que depende da fonte da enzima, do solvente e da reação avaliada. Nesse sentido, o objetivo desta pesquisa fundamenta-se no estudo da cinética de lipase solúvel NS-40116, uma formulação líquida da alteração genética de lipase Thermomyces lanuginosus na reação de transesterificação de óleo de soja refinado e álcool etílico para o desenvolvimento de um modelo mecanístico que possa descrever seu comportamento catalítico assumindo uma mistura de reação heterogênea. As reações foram realizadas a 35°C e em presença de 10%w/wóleo água. O planejamento das reações foi feito mudando as condições de operação: velocidade de agitação (800-1200 RPM), concentração de enzima (0.5 – 2.0%w/wóleo) e conteúdo do álcool (1.5 – 2.0 eq.). Além disso, foram determinadas a relação entre a velocidade de agitação e a razão volumétrica dos substratos com a área interfacial da emulsão óleo-água-álcool. A lipase solúvel NS-40116 foi caracterizada em função do conteúdo de proteínas (31.454±0.002 mg proteína/ml lipase), atividade hidrolítica (48048±653 LU/ml onde 1 LU é a atividade requerida para produzir 1 μmol/min sob condições padrão) e massa molecular (31 kDa). Obteve-se um biodiesel com uma concentração dos ésteres de 82.55±7.17% a partir de óleo de soja refinado (T= 35°C, 800 RPM, 10%w/wóleo água, 2.0%w/wóleo lipase e 2,0 eq. álcool etílico). Foi observado que o diâmetro da gota da emulsão estudada aumenta com o aumento do volume da fase polar (água-álcool) mas diminui com o aumento da velocidade de agitação, afetando inversamente a área interfacial. Foram estimados os parâmetros cinéticos para o modelo matemático proposto que pode descrever a síntese enzimática de biodiesel etanólico utilizando a lipase solúvel NS-40116.Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)CAPES Código de Financiamento 001FAPESP 2016/10636-8porUniversidade Federal de São CarlosCâmpus São CarlosPrograma de Pós-Graduação em Engenharia Química - PPGEQUFSCarBiodieselCinéticaTransesterificação enzimáticaÁrea interfacialLipase solúvelKineticsEnzymatic transesterificationSoluble lipaseInterfacial areaENGENHARIAS::ENGENHARIA QUIMICA::PROCESSOS INDUSTRIAIS DE ENGENHARIA QUIMICAModelagem fenomenológica da síntese enzimática de biodiesel etanólico utilizando lipase solúvelPhenomenological modelling of the synthesis of ethyl biodiesel using soluble lipaseinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/masterThesisOnline600f459889e-82d5-45b8-9703-0d4926219d13info:eu-repo/semantics/openAccessreponame:Repositório Institucional da UFSCARinstname:Universidade Federal de São Carlos (UFSCAR)instacron:UFSCARORIGINALDissertação_FINAL.docx.pdfDissertação_FINAL.docx.pdfapplication/pdf4159740https://repositorio.ufscar.br/bitstream/ufscar/11804/1/Dissertac%cc%a7a%cc%83o_FINAL.docx.pdffe86cd18367e76a2997c7c0c3671ce9dMD51Carta_ProfMarcelo_Dissertaçao.pdfCarta_ProfMarcelo_Dissertaçao.pdfapplication/pdf535256https://repositorio.ufscar.br/bitstream/ufscar/11804/2/Carta_ProfMarcelo_Disserta%c3%a7ao.pdf1414221cfcb204fd9c3909997696aa0cMD52LICENSElicense.txtlicense.txttext/plain; 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dc.title.por.fl_str_mv Modelagem fenomenológica da síntese enzimática de biodiesel etanólico utilizando lipase solúvel
dc.title.alternative.eng.fl_str_mv Phenomenological modelling of the synthesis of ethyl biodiesel using soluble lipase
title Modelagem fenomenológica da síntese enzimática de biodiesel etanólico utilizando lipase solúvel
spellingShingle Modelagem fenomenológica da síntese enzimática de biodiesel etanólico utilizando lipase solúvel
Villegas Aguilar, María Carlota
Biodiesel
Cinética
Transesterificação enzimática
Área interfacial
Lipase solúvel
Kinetics
Enzymatic transesterification
Soluble lipase
Interfacial area
ENGENHARIAS::ENGENHARIA QUIMICA::PROCESSOS INDUSTRIAIS DE ENGENHARIA QUIMICA
title_short Modelagem fenomenológica da síntese enzimática de biodiesel etanólico utilizando lipase solúvel
title_full Modelagem fenomenológica da síntese enzimática de biodiesel etanólico utilizando lipase solúvel
title_fullStr Modelagem fenomenológica da síntese enzimática de biodiesel etanólico utilizando lipase solúvel
title_full_unstemmed Modelagem fenomenológica da síntese enzimática de biodiesel etanólico utilizando lipase solúvel
title_sort Modelagem fenomenológica da síntese enzimática de biodiesel etanólico utilizando lipase solúvel
author Villegas Aguilar, María Carlota
author_facet Villegas Aguilar, María Carlota
author_role author
dc.contributor.authorlattes.por.fl_str_mv http://lattes.cnpq.br/3753884975348864
dc.contributor.author.fl_str_mv Villegas Aguilar, María Carlota
dc.contributor.advisor1.fl_str_mv Ribeiro, Marcelo Perencin de Arruda
dc.contributor.advisor1Lattes.fl_str_mv http://lattes.cnpq.br/0381402687491195
dc.contributor.advisor-co1.fl_str_mv Giordano, Roberto de Campos
dc.contributor.advisor-co1Lattes.fl_str_mv http://lattes.cnpq.br/0834668419587001
dc.contributor.authorID.fl_str_mv e44c2c4d-42d1-42b7-b963-afd00d53f782
contributor_str_mv Ribeiro, Marcelo Perencin de Arruda
Giordano, Roberto de Campos
dc.subject.por.fl_str_mv Biodiesel
Cinética
Transesterificação enzimática
Área interfacial
Lipase solúvel
topic Biodiesel
Cinética
Transesterificação enzimática
Área interfacial
Lipase solúvel
Kinetics
Enzymatic transesterification
Soluble lipase
Interfacial area
ENGENHARIAS::ENGENHARIA QUIMICA::PROCESSOS INDUSTRIAIS DE ENGENHARIA QUIMICA
dc.subject.eng.fl_str_mv Kinetics
Enzymatic transesterification
Soluble lipase
Interfacial area
dc.subject.cnpq.fl_str_mv ENGENHARIAS::ENGENHARIA QUIMICA::PROCESSOS INDUSTRIAIS DE ENGENHARIA QUIMICA
description The kinetics study of the synthesis of ethyl biodiesel allows a deeper understanding of the enzymatic process, providing an important tool for process design, optimization and control. Most of the models proposed in the literature for enzymatic biodiesel production use methanol and immobilized lipases. Moreover, depending on the source of the lipase and the reaction medium, the reaction may have a distinct mechanism. In this work we study the biodiesel production by transesterification of refined soybean oil and bioethanol using the soluble lipase NS-40116, a liquid formulation of a genetic modified lipase from Thermomyces lanuginosus. The aim of this research is to develop a phenomenological model capable of describing the catalytic behavior of that lipase formulation in this heterogeneous medium. Batch assays were carried out in a bench jacketed glass reactor where several process variables were varied: agitation speed (800-1200 rpm), enzyme concentration (0.5-2.0%w/woil) and alcohol content (1.5-2.0 equivalent). All assays were carried out at 35°C with 10%w/woil of water. In addition, the relationship between the agitation speed and the volumetric flow rate of the substrates with the oil-water-alcohol emulsion interface was determined. The soluble lipase NS-40116 was characterized: protein content 31.454 ± 0.002 mg protein/ml lipase, hydrolytic activity 48048 ± 653 LU/ml (1 LU: activity required to produce 1 μmol/min with standard conditions) and molecular weight 31 kDa. An ethyl biodiesel was obtained from refined soybean oil with a concentration of esters: 82.55 ± 7.17% (T = 35°C, 800 RPM, 10%w/woil water, 2.0%w/woil lipase and 2.0 eq. ethyl alcohol). The average interfacial area was evaluated by measuring droplet diameters distribution in pictures of the emulsion obtained in a microscope. Different agitation speeds and polar/nonpolar volume ratios were used. Results show that the average diameter of the droplets increases when the polar volume increases and decreases with the agitation speed. The kinetic parameters were determined for the mathematical model of the enzymatic synthesis of ethyl biodiesel using the soluble lipase NS-40116.
publishDate 2018
dc.date.issued.fl_str_mv 2018-03-27
dc.date.accessioned.fl_str_mv 2019-09-09T17:07:41Z
dc.date.available.fl_str_mv 2019-09-09T17:07:41Z
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dc.identifier.citation.fl_str_mv VILLEGAS AGUILAR, María Carlota. Modelagem fenomenológica da síntese enzimática de biodiesel etanólico utilizando lipase solúvel. 2018. Dissertação (Mestrado em Engenharia Química) – Universidade Federal de São Carlos, São Carlos, 2018. Disponível em: https://repositorio.ufscar.br/handle/ufscar/11804.
dc.identifier.uri.fl_str_mv https://repositorio.ufscar.br/handle/ufscar/11804
identifier_str_mv VILLEGAS AGUILAR, María Carlota. Modelagem fenomenológica da síntese enzimática de biodiesel etanólico utilizando lipase solúvel. 2018. Dissertação (Mestrado em Engenharia Química) – Universidade Federal de São Carlos, São Carlos, 2018. Disponível em: https://repositorio.ufscar.br/handle/ufscar/11804.
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Câmpus São Carlos
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publisher.none.fl_str_mv Universidade Federal de São Carlos
Câmpus São Carlos
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