A BIDISPERSE MODEL TO STUDY THE HYDROLYSIS OF MALTOSE USING GLUCOAMYLASE IMMOBILIZED IN SILICA AND WRAPPED IN PECTIN GEL
Autor(a) principal: | |
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Data de Publicação: | 1997 |
Outros Autores: | , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Brazilian Journal of Chemical Engineering |
Texto Completo: | http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0104-66321997000400006 |
Resumo: | In this work, a bidisperse model is built to represent the hydrolysis of maltose using immobilized glucoamylase. The experimental set is a mixed-batch reactor, maintained at 30ºC, with pectin gel spherical particles that contain enzyme immobilized in macroporous silica. The possibility of substrate adsorption on the pectin gel is also studied because this phenomenon may result in smaller values of diffusivity. Equilibrium assays are then performed for different substrates (maltose, lactose and glucose) at different temperatures and pHs. These assays show that adsorption on the pectin gel is not important for the three dextrins analysed. The bidisperse model presents a good fit with the experimental data, when using previously-estimated kinetic and mass transfer parameters (Gonçalves et al., 1997). This result shows that the methodology used (wrapping the silica in pectin gel) is appropriate for experimental studies with silica, since it allows a higher degree of agitation without causing shearing |
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Brazilian Journal of Chemical Engineering |
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A BIDISPERSE MODEL TO STUDY THE HYDROLYSIS OF MALTOSE USING GLUCOAMYLASE IMMOBILIZED IN SILICA AND WRAPPED IN PECTIN GELMathematical modelsmaltose hydrolysisprocess simulationIn this work, a bidisperse model is built to represent the hydrolysis of maltose using immobilized glucoamylase. The experimental set is a mixed-batch reactor, maintained at 30ºC, with pectin gel spherical particles that contain enzyme immobilized in macroporous silica. The possibility of substrate adsorption on the pectin gel is also studied because this phenomenon may result in smaller values of diffusivity. Equilibrium assays are then performed for different substrates (maltose, lactose and glucose) at different temperatures and pHs. These assays show that adsorption on the pectin gel is not important for the three dextrins analysed. The bidisperse model presents a good fit with the experimental data, when using previously-estimated kinetic and mass transfer parameters (Gonçalves et al., 1997). This result shows that the methodology used (wrapping the silica in pectin gel) is appropriate for experimental studies with silica, since it allows a higher degree of agitation without causing shearingBrazilian Society of Chemical Engineering1997-12-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S0104-66321997000400006Brazilian Journal of Chemical Engineering v.14 n.4 1997reponame:Brazilian Journal of Chemical Engineeringinstname:Associação Brasileira de Engenharia Química (ABEQ)instacron:ABEQ10.1590/S0104-66321997000400006info:eu-repo/semantics/openAccessGonçalves,L.R.B.Giordano,R.L.C.Giordano,R.C.eng1998-10-06T00:00:00Zoai:scielo:S0104-66321997000400006Revistahttps://www.scielo.br/j/bjce/https://old.scielo.br/oai/scielo-oai.phprgiudici@usp.br||rgiudici@usp.br1678-43830104-6632opendoar:1998-10-06T00:00Brazilian Journal of Chemical Engineering - Associação Brasileira de Engenharia Química (ABEQ)false |
dc.title.none.fl_str_mv |
A BIDISPERSE MODEL TO STUDY THE HYDROLYSIS OF MALTOSE USING GLUCOAMYLASE IMMOBILIZED IN SILICA AND WRAPPED IN PECTIN GEL |
title |
A BIDISPERSE MODEL TO STUDY THE HYDROLYSIS OF MALTOSE USING GLUCOAMYLASE IMMOBILIZED IN SILICA AND WRAPPED IN PECTIN GEL |
spellingShingle |
A BIDISPERSE MODEL TO STUDY THE HYDROLYSIS OF MALTOSE USING GLUCOAMYLASE IMMOBILIZED IN SILICA AND WRAPPED IN PECTIN GEL Gonçalves,L.R.B. Mathematical models maltose hydrolysis process simulation |
title_short |
A BIDISPERSE MODEL TO STUDY THE HYDROLYSIS OF MALTOSE USING GLUCOAMYLASE IMMOBILIZED IN SILICA AND WRAPPED IN PECTIN GEL |
title_full |
A BIDISPERSE MODEL TO STUDY THE HYDROLYSIS OF MALTOSE USING GLUCOAMYLASE IMMOBILIZED IN SILICA AND WRAPPED IN PECTIN GEL |
title_fullStr |
A BIDISPERSE MODEL TO STUDY THE HYDROLYSIS OF MALTOSE USING GLUCOAMYLASE IMMOBILIZED IN SILICA AND WRAPPED IN PECTIN GEL |
title_full_unstemmed |
A BIDISPERSE MODEL TO STUDY THE HYDROLYSIS OF MALTOSE USING GLUCOAMYLASE IMMOBILIZED IN SILICA AND WRAPPED IN PECTIN GEL |
title_sort |
A BIDISPERSE MODEL TO STUDY THE HYDROLYSIS OF MALTOSE USING GLUCOAMYLASE IMMOBILIZED IN SILICA AND WRAPPED IN PECTIN GEL |
author |
Gonçalves,L.R.B. |
author_facet |
Gonçalves,L.R.B. Giordano,R.L.C. Giordano,R.C. |
author_role |
author |
author2 |
Giordano,R.L.C. Giordano,R.C. |
author2_role |
author author |
dc.contributor.author.fl_str_mv |
Gonçalves,L.R.B. Giordano,R.L.C. Giordano,R.C. |
dc.subject.por.fl_str_mv |
Mathematical models maltose hydrolysis process simulation |
topic |
Mathematical models maltose hydrolysis process simulation |
description |
In this work, a bidisperse model is built to represent the hydrolysis of maltose using immobilized glucoamylase. The experimental set is a mixed-batch reactor, maintained at 30ºC, with pectin gel spherical particles that contain enzyme immobilized in macroporous silica. The possibility of substrate adsorption on the pectin gel is also studied because this phenomenon may result in smaller values of diffusivity. Equilibrium assays are then performed for different substrates (maltose, lactose and glucose) at different temperatures and pHs. These assays show that adsorption on the pectin gel is not important for the three dextrins analysed. The bidisperse model presents a good fit with the experimental data, when using previously-estimated kinetic and mass transfer parameters (Gonçalves et al., 1997). This result shows that the methodology used (wrapping the silica in pectin gel) is appropriate for experimental studies with silica, since it allows a higher degree of agitation without causing shearing |
publishDate |
1997 |
dc.date.none.fl_str_mv |
1997-12-01 |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0104-66321997000400006 |
url |
http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0104-66321997000400006 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
10.1590/S0104-66321997000400006 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
text/html |
dc.publisher.none.fl_str_mv |
Brazilian Society of Chemical Engineering |
publisher.none.fl_str_mv |
Brazilian Society of Chemical Engineering |
dc.source.none.fl_str_mv |
Brazilian Journal of Chemical Engineering v.14 n.4 1997 reponame:Brazilian Journal of Chemical Engineering instname:Associação Brasileira de Engenharia Química (ABEQ) instacron:ABEQ |
instname_str |
Associação Brasileira de Engenharia Química (ABEQ) |
instacron_str |
ABEQ |
institution |
ABEQ |
reponame_str |
Brazilian Journal of Chemical Engineering |
collection |
Brazilian Journal of Chemical Engineering |
repository.name.fl_str_mv |
Brazilian Journal of Chemical Engineering - Associação Brasileira de Engenharia Química (ABEQ) |
repository.mail.fl_str_mv |
rgiudici@usp.br||rgiudici@usp.br |
_version_ |
1754213170308710400 |