Stabilization of penicillin G acylase by immobilization on glutaraldehyde-activated chitosan
Autor(a) principal: | |
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Data de Publicação: | 2005 |
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=S0104-66322005000400005 |
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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Brazilian Journal of Chemical Engineering |
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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 |
_version_ |
1754213171924566016 |