Comparação de diferentes modelos de reatores para a hidrólise enzimática da sacarose

Detalhes bibliográficos
Autor(a) principal: Rodríguez, Miguel Angel Aparicio
Data de Publicação: 1998
Tipo de documento: Dissertação
Idioma: por
Título da fonte: Repositório Institucional da Universidade Estadual de Maringá (RI-UEM)
Texto Completo: http://repositorio.uem.br:8080/jspui/handle/1/3719
Resumo: The objective of this work consisted in evaluating the performance of a given set of continuous ideal reactors models, aiming at the identification of which model gives the smallest space time for the production of inverted sugar by enzymatic hydrolysis of sucrose. Reactor conditions were: 850 g/L of sucrose, pH 5, 55º C, 0.1698 g/L of Novo Nordisk invertase and final conversion of 98%. The adopted kinetic model includes inhibition by the substrate (sucrose) and product (glucose + fructose), variation of water concentration, and enzyme thermal deactivation. The space time was calculated by coupling the kinetic rate expression with the design equation for ideal reactors. The resulting mathematical models were solved with the software called Derive. Disregarding enzyme thermal deactivation, the system CSTR+PFR requires the smallest space time (11.7000 h), while the second best choice is a single PFR (t = 11.7056 h). A single CSTR requires the largest space time, namely 114.43 h. The inclusion of thermal deactivation of the enzyme in the analysis has allowed to conclude that with a single CSTR it is impossible to reach the conversion of 98%, for the specified reactor conditions, unless the enzyme charge is increased. With the system CSTR+PFR it was possible to reach the final conversion of 98%, if the conversion of the CSTR was lower than 89.72%. With the recycle tubular reactor the conversion reaches 98% only for recycle ratios in the range of zero to .003, and as R →2,003, t → ∞. The reactor model with the minimum space time in the presence of enzyme deactivation is a single PFR with t= 16.9554 h. Therefore, product inhibition, in the case of high sucrose concentration and conversion, is a critical factor for the performance of the hydrolysis reactor. Neglecting invertase thermal deactivation leads to significant errors of undersizing the reactors, in addition to pointing to the wrong optimal reactor system.
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spelling Comparação de diferentes modelos de reatores para a hidrólise enzimática da sacaroseComparison of different reactor models for enzymatic hydrolysis of sucrose.BioengenhariaDesenvolvimento de reatores de processosHidrólise enzimática da sacaroseBiorreatorBrasil.EngenhariasEngenharia QuímicaThe objective of this work consisted in evaluating the performance of a given set of continuous ideal reactors models, aiming at the identification of which model gives the smallest space time for the production of inverted sugar by enzymatic hydrolysis of sucrose. Reactor conditions were: 850 g/L of sucrose, pH 5, 55º C, 0.1698 g/L of Novo Nordisk invertase and final conversion of 98%. The adopted kinetic model includes inhibition by the substrate (sucrose) and product (glucose + fructose), variation of water concentration, and enzyme thermal deactivation. The space time was calculated by coupling the kinetic rate expression with the design equation for ideal reactors. The resulting mathematical models were solved with the software called Derive. Disregarding enzyme thermal deactivation, the system CSTR+PFR requires the smallest space time (11.7000 h), while the second best choice is a single PFR (t = 11.7056 h). A single CSTR requires the largest space time, namely 114.43 h. The inclusion of thermal deactivation of the enzyme in the analysis has allowed to conclude that with a single CSTR it is impossible to reach the conversion of 98%, for the specified reactor conditions, unless the enzyme charge is increased. With the system CSTR+PFR it was possible to reach the final conversion of 98%, if the conversion of the CSTR was lower than 89.72%. With the recycle tubular reactor the conversion reaches 98% only for recycle ratios in the range of zero to .003, and as R →2,003, t → ∞. The reactor model with the minimum space time in the presence of enzyme deactivation is a single PFR with t= 16.9554 h. Therefore, product inhibition, in the case of high sucrose concentration and conversion, is a critical factor for the performance of the hydrolysis reactor. Neglecting invertase thermal deactivation leads to significant errors of undersizing the reactors, in addition to pointing to the wrong optimal reactor system.O objetivo deste trabalho consistiu em avaliar o desempenho de um conjunto de modelos de reatores ideais contínuos visando determinar-se o modelo de menor tempo espacial para a produção de açúcar invertido, por hidrólise enzimática de sacarose à 850 g/L, pH 5, 55 °C, com 0,1698 g/L de invertase Novo Nordisk e conversão final de 98%. O modelo da cinética de hidrólise incluiu a inibição pelo substrato (sacarose) e pelo produto (glicose + frutose), a variação da concentração da água, e a desnaturação térmica da enzima. O tempo espacial foi calculado pelo acoplamento da equação cinética e das equações de projeto dos reatores ideais, sendo os modelos matemáticos resultantes resolvidos pelo programa DERIVE. Desconsiderando-se a desnaturação térmica da enzima, o sistema CSTR + PFR exige o menor tempo espacial (11,7000 h), enquanto a segunda opção recaiu sobre um único PFR (t = 11,7056 h). Um único CSTR exige o maior tempo espacial, 114,4300 h. A inclusão da desnaturação térmica da enzima na análise permitiu concluir que, com um único CSTR, não é possível alcançar-se a conversão de 98%, para as condições usadas, a não ser que a quantidade de enzima seja aumentada. Com o sistema CSTR + PFR foi possível alcançar-se a conversão final de 98%, desde que a conversão do CSTR seja inferior a 89,72%. Com o Reator Tubular de Reciclo a conversão alcança 98% apenas para razões de reciclo entre O e 2,003, e quando R →2,003, t → ∞. O modelo de reator de menor tempo espacial com desnaturação da enzima, é um único PER, com t = 16,9554 h. Portanto, conclui-se que a inibição pelo produto, para altas concentrações de sacarose, e altas conversões, é o fator critico para o desempenho dos reatores. A desconsideração do fenômeno de desnaturação térmica da invertase conduz a erros significativos de subdimensionamento, além de indicar erroneamente qual é o melhor modelo de reator.130 pUniversidade Estadual de MaringáBrasilDepartamento de Engenharia QuímicaPrograma de Pós-Graduação em Engenharia QuímicaUEMMaringá, PRCentro de TecnologiaFlávio Faria de MoraesGisella Maria Zanin - UEMMarcos de Souza - UEMJosé Eduardo Olivo - UEMRodríguez, Miguel Angel Aparicio2018-04-17T17:42:52Z2018-04-17T17:42:52Z1998info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/masterThesishttp://repositorio.uem.br:8080/jspui/handle/1/3719porinfo:eu-repo/semantics/openAccessreponame:Repositório Institucional da Universidade Estadual de Maringá (RI-UEM)instname:Universidade Estadual de Maringá (UEM)instacron:UEM2024-03-25T19:45:33Zoai:localhost:1/3719Repositório InstitucionalPUBhttp://repositorio.uem.br:8080/oai/requestopendoar:2024-04-23T14:56:52.334405Repositório Institucional da Universidade Estadual de Maringá (RI-UEM) - Universidade Estadual de Maringá (UEM)false
dc.title.none.fl_str_mv Comparação de diferentes modelos de reatores para a hidrólise enzimática da sacarose
Comparison of different reactor models for enzymatic hydrolysis of sucrose.
title Comparação de diferentes modelos de reatores para a hidrólise enzimática da sacarose
spellingShingle Comparação de diferentes modelos de reatores para a hidrólise enzimática da sacarose
Rodríguez, Miguel Angel Aparicio
Bioengenharia
Desenvolvimento de reatores de processos
Hidrólise enzimática da sacarose
Biorreator
Brasil.
Engenharias
Engenharia Química
title_short Comparação de diferentes modelos de reatores para a hidrólise enzimática da sacarose
title_full Comparação de diferentes modelos de reatores para a hidrólise enzimática da sacarose
title_fullStr Comparação de diferentes modelos de reatores para a hidrólise enzimática da sacarose
title_full_unstemmed Comparação de diferentes modelos de reatores para a hidrólise enzimática da sacarose
title_sort Comparação de diferentes modelos de reatores para a hidrólise enzimática da sacarose
author Rodríguez, Miguel Angel Aparicio
author_facet Rodríguez, Miguel Angel Aparicio
author_role author
dc.contributor.none.fl_str_mv Flávio Faria de Moraes
Gisella Maria Zanin - UEM
Marcos de Souza - UEM
José Eduardo Olivo - UEM
dc.contributor.author.fl_str_mv Rodríguez, Miguel Angel Aparicio
dc.subject.por.fl_str_mv Bioengenharia
Desenvolvimento de reatores de processos
Hidrólise enzimática da sacarose
Biorreator
Brasil.
Engenharias
Engenharia Química
topic Bioengenharia
Desenvolvimento de reatores de processos
Hidrólise enzimática da sacarose
Biorreator
Brasil.
Engenharias
Engenharia Química
description The objective of this work consisted in evaluating the performance of a given set of continuous ideal reactors models, aiming at the identification of which model gives the smallest space time for the production of inverted sugar by enzymatic hydrolysis of sucrose. Reactor conditions were: 850 g/L of sucrose, pH 5, 55º C, 0.1698 g/L of Novo Nordisk invertase and final conversion of 98%. The adopted kinetic model includes inhibition by the substrate (sucrose) and product (glucose + fructose), variation of water concentration, and enzyme thermal deactivation. The space time was calculated by coupling the kinetic rate expression with the design equation for ideal reactors. The resulting mathematical models were solved with the software called Derive. Disregarding enzyme thermal deactivation, the system CSTR+PFR requires the smallest space time (11.7000 h), while the second best choice is a single PFR (t = 11.7056 h). A single CSTR requires the largest space time, namely 114.43 h. The inclusion of thermal deactivation of the enzyme in the analysis has allowed to conclude that with a single CSTR it is impossible to reach the conversion of 98%, for the specified reactor conditions, unless the enzyme charge is increased. With the system CSTR+PFR it was possible to reach the final conversion of 98%, if the conversion of the CSTR was lower than 89.72%. With the recycle tubular reactor the conversion reaches 98% only for recycle ratios in the range of zero to .003, and as R →2,003, t → ∞. The reactor model with the minimum space time in the presence of enzyme deactivation is a single PFR with t= 16.9554 h. Therefore, product inhibition, in the case of high sucrose concentration and conversion, is a critical factor for the performance of the hydrolysis reactor. Neglecting invertase thermal deactivation leads to significant errors of undersizing the reactors, in addition to pointing to the wrong optimal reactor system.
publishDate 1998
dc.date.none.fl_str_mv 1998
2018-04-17T17:42:52Z
2018-04-17T17:42:52Z
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/masterThesis
format masterThesis
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://repositorio.uem.br:8080/jspui/handle/1/3719
url http://repositorio.uem.br:8080/jspui/handle/1/3719
dc.language.iso.fl_str_mv por
language por
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.publisher.none.fl_str_mv Universidade Estadual de Maringá
Brasil
Departamento de Engenharia Química
Programa de Pós-Graduação em Engenharia Química
UEM
Maringá, PR
Centro de Tecnologia
publisher.none.fl_str_mv Universidade Estadual de Maringá
Brasil
Departamento de Engenharia Química
Programa de Pós-Graduação em Engenharia Química
UEM
Maringá, PR
Centro de Tecnologia
dc.source.none.fl_str_mv reponame:Repositório Institucional da Universidade Estadual de Maringá (RI-UEM)
instname:Universidade Estadual de Maringá (UEM)
instacron:UEM
instname_str Universidade Estadual de Maringá (UEM)
instacron_str UEM
institution UEM
reponame_str Repositório Institucional da Universidade Estadual de Maringá (RI-UEM)
collection Repositório Institucional da Universidade Estadual de Maringá (RI-UEM)
repository.name.fl_str_mv Repositório Institucional da Universidade Estadual de Maringá (RI-UEM) - Universidade Estadual de Maringá (UEM)
repository.mail.fl_str_mv
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