Immobilization of lipase on mesoporous molecular sieve MCM-48 obtained using ionic solid as a structure director and esterification reaction on solvent-free

Detalhes bibliográficos
Autor(a) principal: Battiston,Catia S. Z.
Data de Publicação: 2017
Outros Autores: Ficanha,Aline M. M., Levandoski,Katarine L. D., Silva,Bernardo A. da, Battiston,Suellen, Dallago,Rogério M., Mignoni,Marcelo L.
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Química Nova (Online)
Texto Completo: http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0100-40422017000300293
Resumo: Candida antarctica lipase B (CALB) is an enzyme able to catalyze chemical reaction, however when it is used as a free enzyme, it cannot be recovered from reaction medium. One of the alternatives is to immobilize the enzymes on a support which allows the maintenance of their catalytic activities. The purpose of this paper was to immobilize the CALB on MCM-48 using the ionic solid [C16MI]Cl as structure director. 22 CCRD (Central Composite Rotational Design) was proposed to analyze the influence of the variables like enzyme mass (0.059 to 0.341 g) and ionic solid concentration (0.59 to 3.41%) in the enzyme immobilization process to obtain the maximum esterification activity in order to optimize the process. After immobilization, the study results showed that the enzymes exhibited improvement of thermal (40, 60 and 80 ºC) and storage stability (90 days), besides the possibility to reuse of the enzyme up to 10 times, showing residual activity of 50%.
id SBQ-3_2db55eada4a7d5965087a23fe340c2f3
oai_identifier_str oai:scielo:S0100-40422017000300293
network_acronym_str SBQ-3
network_name_str Química Nova (Online)
repository_id_str
spelling Immobilization of lipase on mesoporous molecular sieve MCM-48 obtained using ionic solid as a structure director and esterification reaction on solvent-freelipaseimmobilizationMCM-48ionic solidCandida antarctica lipase B (CALB) is an enzyme able to catalyze chemical reaction, however when it is used as a free enzyme, it cannot be recovered from reaction medium. One of the alternatives is to immobilize the enzymes on a support which allows the maintenance of their catalytic activities. The purpose of this paper was to immobilize the CALB on MCM-48 using the ionic solid [C16MI]Cl as structure director. 22 CCRD (Central Composite Rotational Design) was proposed to analyze the influence of the variables like enzyme mass (0.059 to 0.341 g) and ionic solid concentration (0.59 to 3.41%) in the enzyme immobilization process to obtain the maximum esterification activity in order to optimize the process. After immobilization, the study results showed that the enzymes exhibited improvement of thermal (40, 60 and 80 ºC) and storage stability (90 days), besides the possibility to reuse of the enzyme up to 10 times, showing residual activity of 50%.Sociedade Brasileira de Química2017-04-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S0100-40422017000300293Química Nova v.40 n.3 2017reponame:Química Nova (Online)instname:Sociedade Brasileira de Química (SBQ)instacron:SBQ10.21577/0100-4042.20170011info:eu-repo/semantics/openAccessBattiston,Catia S. Z.Ficanha,Aline M. M.Levandoski,Katarine L. D.Silva,Bernardo A. daBattiston,SuellenDallago,Rogério M.Mignoni,Marcelo L.eng2017-05-05T00:00:00Zoai:scielo:S0100-40422017000300293Revistahttps://www.scielo.br/j/qn/ONGhttps://old.scielo.br/oai/scielo-oai.phpquimicanova@sbq.org.br1678-70640100-4042opendoar:2017-05-05T00:00Química Nova (Online) - Sociedade Brasileira de Química (SBQ)false
dc.title.none.fl_str_mv Immobilization of lipase on mesoporous molecular sieve MCM-48 obtained using ionic solid as a structure director and esterification reaction on solvent-free
title Immobilization of lipase on mesoporous molecular sieve MCM-48 obtained using ionic solid as a structure director and esterification reaction on solvent-free
spellingShingle Immobilization of lipase on mesoporous molecular sieve MCM-48 obtained using ionic solid as a structure director and esterification reaction on solvent-free
Battiston,Catia S. Z.
lipase
immobilization
MCM-48
ionic solid
title_short Immobilization of lipase on mesoporous molecular sieve MCM-48 obtained using ionic solid as a structure director and esterification reaction on solvent-free
title_full Immobilization of lipase on mesoporous molecular sieve MCM-48 obtained using ionic solid as a structure director and esterification reaction on solvent-free
title_fullStr Immobilization of lipase on mesoporous molecular sieve MCM-48 obtained using ionic solid as a structure director and esterification reaction on solvent-free
title_full_unstemmed Immobilization of lipase on mesoporous molecular sieve MCM-48 obtained using ionic solid as a structure director and esterification reaction on solvent-free
title_sort Immobilization of lipase on mesoporous molecular sieve MCM-48 obtained using ionic solid as a structure director and esterification reaction on solvent-free
author Battiston,Catia S. Z.
author_facet Battiston,Catia S. Z.
Ficanha,Aline M. M.
Levandoski,Katarine L. D.
Silva,Bernardo A. da
Battiston,Suellen
Dallago,Rogério M.
Mignoni,Marcelo L.
author_role author
author2 Ficanha,Aline M. M.
Levandoski,Katarine L. D.
Silva,Bernardo A. da
Battiston,Suellen
Dallago,Rogério M.
Mignoni,Marcelo L.
author2_role author
author
author
author
author
author
dc.contributor.author.fl_str_mv Battiston,Catia S. Z.
Ficanha,Aline M. M.
Levandoski,Katarine L. D.
Silva,Bernardo A. da
Battiston,Suellen
Dallago,Rogério M.
Mignoni,Marcelo L.
dc.subject.por.fl_str_mv lipase
immobilization
MCM-48
ionic solid
topic lipase
immobilization
MCM-48
ionic solid
description Candida antarctica lipase B (CALB) is an enzyme able to catalyze chemical reaction, however when it is used as a free enzyme, it cannot be recovered from reaction medium. One of the alternatives is to immobilize the enzymes on a support which allows the maintenance of their catalytic activities. The purpose of this paper was to immobilize the CALB on MCM-48 using the ionic solid [C16MI]Cl as structure director. 22 CCRD (Central Composite Rotational Design) was proposed to analyze the influence of the variables like enzyme mass (0.059 to 0.341 g) and ionic solid concentration (0.59 to 3.41%) in the enzyme immobilization process to obtain the maximum esterification activity in order to optimize the process. After immobilization, the study results showed that the enzymes exhibited improvement of thermal (40, 60 and 80 ºC) and storage stability (90 days), besides the possibility to reuse of the enzyme up to 10 times, showing residual activity of 50%.
publishDate 2017
dc.date.none.fl_str_mv 2017-04-01
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=S0100-40422017000300293
url http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0100-40422017000300293
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 10.21577/0100-4042.20170011
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 Sociedade Brasileira de Química
publisher.none.fl_str_mv Sociedade Brasileira de Química
dc.source.none.fl_str_mv Química Nova v.40 n.3 2017
reponame:Química Nova (Online)
instname:Sociedade Brasileira de Química (SBQ)
instacron:SBQ
instname_str Sociedade Brasileira de Química (SBQ)
instacron_str SBQ
institution SBQ
reponame_str Química Nova (Online)
collection Química Nova (Online)
repository.name.fl_str_mv Química Nova (Online) - Sociedade Brasileira de Química (SBQ)
repository.mail.fl_str_mv quimicanova@sbq.org.br
_version_ 1750318118007209984

Registros relacionados