Stabilization of penicillin G acylase by immobilization on glutaraldehyde-activated chitosan

Detalhes bibliográficos
Autor(a) principal: Adriano,W. S.
Data de Publicação: 2005
Outros Autores: Filho,E. H. C., Silva,J. A., Giordano,R. L. C., Gonçalves,L. R.B.
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=S0104-66322005000400005
Resumo: The objective of this work was to study enzyme immobilization on chitosan activated with glutaraldehyde, aiming to produce a cheap biocatalyst. Two different immobilization strategies were studied: one-point and multipoint covalent attachment to the solid matrix. The multipoint covalent attachment derivative had an 82% immobilization yield. It was 4.9-fold more stable than the free enzyme at 50°C and 4.5-fold more stable than soluble enzyme at pH 10.0. The one-point derivative had an 85% immobilization yield. It was 2.7-fold more stable than the free enzyme at 50°C and 3.8-fold more stable than soluble PGA at pH 10.0. Results indicated that chitosan can be loaded with PGA above 330 IU/g. Intraparticle diffusive effects, however, limited hydrolysis of penicillin G catalyzed by those derivatives at 37°C and 25°C. Operational stability assays were performed and the multipoint derivative exhibited a half-life of 40 hours.
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spelling Stabilization of penicillin G acylase by immobilization on glutaraldehyde-activated chitosanStabilization of enzymesPenicillin G acylaseChitosan and immobilization of enzymesThe objective of this work was to study enzyme immobilization on chitosan activated with glutaraldehyde, aiming to produce a cheap biocatalyst. Two different immobilization strategies were studied: one-point and multipoint covalent attachment to the solid matrix. The multipoint covalent attachment derivative had an 82% immobilization yield. It was 4.9-fold more stable than the free enzyme at 50°C and 4.5-fold more stable than soluble enzyme at pH 10.0. The one-point derivative had an 85% immobilization yield. It was 2.7-fold more stable than the free enzyme at 50°C and 3.8-fold more stable than soluble PGA at pH 10.0. Results indicated that chitosan can be loaded with PGA above 330 IU/g. Intraparticle diffusive effects, however, limited hydrolysis of penicillin G catalyzed by those derivatives at 37°C and 25°C. Operational stability assays were performed and the multipoint derivative exhibited a half-life of 40 hours.Brazilian Society of Chemical Engineering2005-12-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S0104-66322005000400005Brazilian Journal of Chemical Engineering v.22 n.4 2005reponame:Brazilian Journal of Chemical Engineeringinstname:Associação Brasileira de Engenharia Química (ABEQ)instacron:ABEQ10.1590/S0104-66322005000400005info:eu-repo/semantics/openAccessAdriano,W. S.Filho,E. H. C.Silva,J. A.Giordano,R. L. C.Gonçalves,L. R.B.eng2006-01-02T00:00:00Zoai:scielo:S0104-66322005000400005Revistahttps://www.scielo.br/j/bjce/https://old.scielo.br/oai/scielo-oai.phprgiudici@usp.br||rgiudici@usp.br1678-43830104-6632opendoar:2006-01-02T00:00Brazilian Journal of Chemical Engineering - Associação Brasileira de Engenharia Química (ABEQ)false
dc.title.none.fl_str_mv Stabilization of penicillin G acylase by immobilization on glutaraldehyde-activated chitosan
title Stabilization of penicillin G acylase by immobilization on glutaraldehyde-activated chitosan
spellingShingle Stabilization of penicillin G acylase by immobilization on glutaraldehyde-activated chitosan
Adriano,W. S.
Stabilization of enzymes
Penicillin G acylase
Chitosan and immobilization of enzymes
title_short Stabilization of penicillin G acylase by immobilization on glutaraldehyde-activated chitosan
title_full Stabilization of penicillin G acylase by immobilization on glutaraldehyde-activated chitosan
title_fullStr Stabilization of penicillin G acylase by immobilization on glutaraldehyde-activated chitosan
title_full_unstemmed Stabilization of penicillin G acylase by immobilization on glutaraldehyde-activated chitosan
title_sort Stabilization of penicillin G acylase by immobilization on glutaraldehyde-activated chitosan
author Adriano,W. S.
author_facet Adriano,W. S.
Filho,E. H. C.
Silva,J. A.
Giordano,R. L. C.
Gonçalves,L. R.B.
author_role author
author2 Filho,E. H. C.
Silva,J. A.
Giordano,R. L. C.
Gonçalves,L. R.B.
author2_role author
author
author
author
dc.contributor.author.fl_str_mv Adriano,W. S.
Filho,E. H. C.
Silva,J. A.
Giordano,R. L. C.
Gonçalves,L. R.B.
dc.subject.por.fl_str_mv Stabilization of enzymes
Penicillin G acylase
Chitosan and immobilization of enzymes
topic Stabilization of enzymes
Penicillin G acylase
Chitosan and immobilization of enzymes
description The objective of this work was to study enzyme immobilization on chitosan activated with glutaraldehyde, aiming to produce a cheap biocatalyst. Two different immobilization strategies were studied: one-point and multipoint covalent attachment to the solid matrix. The multipoint covalent attachment derivative had an 82% immobilization yield. It was 4.9-fold more stable than the free enzyme at 50°C and 4.5-fold more stable than soluble enzyme at pH 10.0. The one-point derivative had an 85% immobilization yield. It was 2.7-fold more stable than the free enzyme at 50°C and 3.8-fold more stable than soluble PGA at pH 10.0. Results indicated that chitosan can be loaded with PGA above 330 IU/g. Intraparticle diffusive effects, however, limited hydrolysis of penicillin G catalyzed by those derivatives at 37°C and 25°C. Operational stability assays were performed and the multipoint derivative exhibited a half-life of 40 hours.
publishDate 2005
dc.date.none.fl_str_mv 2005-12-01
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=S0104-66322005000400005
url http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0104-66322005000400005
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 10.1590/S0104-66322005000400005
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.22 n.4 2005
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
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