IMPROVING THE CATALYTIC FEATURES OF THE LIPASE FROM Rhizomucor miehei IMMOBILIZED ON CHITOSAN-BASED HYBRID MATRICES BY ALTERING THE CHEMICAL ACTIVATION CONDITIONS

Detalhes bibliográficos
Autor(a) principal: Carneiro,Elizabete Araújo
Data de Publicação: 2020
Outros Autores: Bastos,Ana Karine Pessoa, Oliveira,Ulisses Marcondes Freire de, Matos,Leonardo José Brandão Lima de, Adriano,Wellington Sabino, Monteiro,Rodolpho Ramilton de Castro, Santos,José Cleiton Sousa dos, Gonçalves,Luciana Rocha Barros
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Química Nova (Online)
Texto Completo: http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0100-40422020000901234
Resumo: The lipase from Rhizomucor miehei (RML) has been immobilized on chitosan-based hybrid (sodium alginate or carrageenan) matrices activated with glycidol (GLY), epichlorohydrin (EPI) or glutaraldehyde (GLU) groups. Then, the properties of the different biocatalysts have been evaluated and compared with the soluble RML. Thermal stability (at pH 7.0 and 60 °C) was significantly increased when compared to the soluble enzyme: 154-fold for chitosan 5.0% - GLU, 80-fold for chitosan 2.5% - carrageenan 2.5% - GLY and 93-fold for chitosan 2.5% - alginate 2.5% - EPI. The best biocatalyst preparation, which was 154-fold more stable than the soluble enzyme, was obtained when RML was immobilized on chitosan activated with glutaraldehyde 5.0% v/v. According to the results, it was concluded that RML immobilization on chitosan-based hybrid matrices using different chemistries greatly produced biocatalysts with different properties.
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spelling IMPROVING THE CATALYTIC FEATURES OF THE LIPASE FROM Rhizomucor miehei IMMOBILIZED ON CHITOSAN-BASED HYBRID MATRICES BY ALTERING THE CHEMICAL ACTIVATION CONDITIONSbiocatalysts immobilizationlipase stabilizationmodulation of lipaseglycidolglutaraldehydeepichlorohydrinThe lipase from Rhizomucor miehei (RML) has been immobilized on chitosan-based hybrid (sodium alginate or carrageenan) matrices activated with glycidol (GLY), epichlorohydrin (EPI) or glutaraldehyde (GLU) groups. Then, the properties of the different biocatalysts have been evaluated and compared with the soluble RML. Thermal stability (at pH 7.0 and 60 °C) was significantly increased when compared to the soluble enzyme: 154-fold for chitosan 5.0% - GLU, 80-fold for chitosan 2.5% - carrageenan 2.5% - GLY and 93-fold for chitosan 2.5% - alginate 2.5% - EPI. The best biocatalyst preparation, which was 154-fold more stable than the soluble enzyme, was obtained when RML was immobilized on chitosan activated with glutaraldehyde 5.0% v/v. According to the results, it was concluded that RML immobilization on chitosan-based hybrid matrices using different chemistries greatly produced biocatalysts with different properties.Sociedade Brasileira de Química2020-09-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S0100-40422020000901234Química Nova v.43 n.9 2020reponame:Química Nova (Online)instname:Sociedade Brasileira de Química (SBQ)instacron:SBQ10.21577/0100-4042.20170615info:eu-repo/semantics/openAccessCarneiro,Elizabete AraújoBastos,Ana Karine PessoaOliveira,Ulisses Marcondes Freire deMatos,Leonardo José Brandão Lima deAdriano,Wellington SabinoMonteiro,Rodolpho Ramilton de CastroSantos,José Cleiton Sousa dosGonçalves,Luciana Rocha Barroseng2020-10-26T00:00:00Zoai:scielo:S0100-40422020000901234Revistahttps://www.scielo.br/j/qn/ONGhttps://old.scielo.br/oai/scielo-oai.phpquimicanova@sbq.org.br1678-70640100-4042opendoar:2020-10-26T00:00Química Nova (Online) - Sociedade Brasileira de Química (SBQ)false
dc.title.none.fl_str_mv IMPROVING THE CATALYTIC FEATURES OF THE LIPASE FROM Rhizomucor miehei IMMOBILIZED ON CHITOSAN-BASED HYBRID MATRICES BY ALTERING THE CHEMICAL ACTIVATION CONDITIONS
title IMPROVING THE CATALYTIC FEATURES OF THE LIPASE FROM Rhizomucor miehei IMMOBILIZED ON CHITOSAN-BASED HYBRID MATRICES BY ALTERING THE CHEMICAL ACTIVATION CONDITIONS
spellingShingle IMPROVING THE CATALYTIC FEATURES OF THE LIPASE FROM Rhizomucor miehei IMMOBILIZED ON CHITOSAN-BASED HYBRID MATRICES BY ALTERING THE CHEMICAL ACTIVATION CONDITIONS
Carneiro,Elizabete Araújo
biocatalysts immobilization
lipase stabilization
modulation of lipase
glycidol
glutaraldehyde
epichlorohydrin
title_short IMPROVING THE CATALYTIC FEATURES OF THE LIPASE FROM Rhizomucor miehei IMMOBILIZED ON CHITOSAN-BASED HYBRID MATRICES BY ALTERING THE CHEMICAL ACTIVATION CONDITIONS
title_full IMPROVING THE CATALYTIC FEATURES OF THE LIPASE FROM Rhizomucor miehei IMMOBILIZED ON CHITOSAN-BASED HYBRID MATRICES BY ALTERING THE CHEMICAL ACTIVATION CONDITIONS
title_fullStr IMPROVING THE CATALYTIC FEATURES OF THE LIPASE FROM Rhizomucor miehei IMMOBILIZED ON CHITOSAN-BASED HYBRID MATRICES BY ALTERING THE CHEMICAL ACTIVATION CONDITIONS
title_full_unstemmed IMPROVING THE CATALYTIC FEATURES OF THE LIPASE FROM Rhizomucor miehei IMMOBILIZED ON CHITOSAN-BASED HYBRID MATRICES BY ALTERING THE CHEMICAL ACTIVATION CONDITIONS
title_sort IMPROVING THE CATALYTIC FEATURES OF THE LIPASE FROM Rhizomucor miehei IMMOBILIZED ON CHITOSAN-BASED HYBRID MATRICES BY ALTERING THE CHEMICAL ACTIVATION CONDITIONS
author Carneiro,Elizabete Araújo
author_facet Carneiro,Elizabete Araújo
Bastos,Ana Karine Pessoa
Oliveira,Ulisses Marcondes Freire de
Matos,Leonardo José Brandão Lima de
Adriano,Wellington Sabino
Monteiro,Rodolpho Ramilton de Castro
Santos,José Cleiton Sousa dos
Gonçalves,Luciana Rocha Barros
author_role author
author2 Bastos,Ana Karine Pessoa
Oliveira,Ulisses Marcondes Freire de
Matos,Leonardo José Brandão Lima de
Adriano,Wellington Sabino
Monteiro,Rodolpho Ramilton de Castro
Santos,José Cleiton Sousa dos
Gonçalves,Luciana Rocha Barros
author2_role author
author
author
author
author
author
author
dc.contributor.author.fl_str_mv Carneiro,Elizabete Araújo
Bastos,Ana Karine Pessoa
Oliveira,Ulisses Marcondes Freire de
Matos,Leonardo José Brandão Lima de
Adriano,Wellington Sabino
Monteiro,Rodolpho Ramilton de Castro
Santos,José Cleiton Sousa dos
Gonçalves,Luciana Rocha Barros
dc.subject.por.fl_str_mv biocatalysts immobilization
lipase stabilization
modulation of lipase
glycidol
glutaraldehyde
epichlorohydrin
topic biocatalysts immobilization
lipase stabilization
modulation of lipase
glycidol
glutaraldehyde
epichlorohydrin
description The lipase from Rhizomucor miehei (RML) has been immobilized on chitosan-based hybrid (sodium alginate or carrageenan) matrices activated with glycidol (GLY), epichlorohydrin (EPI) or glutaraldehyde (GLU) groups. Then, the properties of the different biocatalysts have been evaluated and compared with the soluble RML. Thermal stability (at pH 7.0 and 60 °C) was significantly increased when compared to the soluble enzyme: 154-fold for chitosan 5.0% - GLU, 80-fold for chitosan 2.5% - carrageenan 2.5% - GLY and 93-fold for chitosan 2.5% - alginate 2.5% - EPI. The best biocatalyst preparation, which was 154-fold more stable than the soluble enzyme, was obtained when RML was immobilized on chitosan activated with glutaraldehyde 5.0% v/v. According to the results, it was concluded that RML immobilization on chitosan-based hybrid matrices using different chemistries greatly produced biocatalysts with different properties.
publishDate 2020
dc.date.none.fl_str_mv 2020-09-01
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=S0100-40422020000901234
url http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0100-40422020000901234
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 10.21577/0100-4042.20170615
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.43 n.9 2020
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
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