Chitosan/siloxane hybrid polymer: synthesis, characterization and performance as a support for immobilizing enzyme
Autor(a) principal: | |
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Data de Publicação: | 2011 |
Outros Autores: | , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Journal of the Brazilian Chemical Society (Online) |
Texto Completo: | http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0103-50532011000800003 |
Resumo: | A hybrid polymer derived from siloxane and chitosan was obtained by sol-gel technique using tetraethoxysilane (TEOS) as a precursor. The hybrid support was chemically modified with epichlorohydrin and used to immobilize lipase from Burkholderia cepacia. The hybrid SiO2-chitosan formed new macromolecular structure in which the inorganic particles are dispersed at the nanometer scale in the organic host matrix and bounding through covalent bonds. A comparative study between free and immobilized lipase was provided in terms of pH, temperature, kinetic parameters and thermal stability. The pH for maximum hydrolysis activity shifted from 7.0 for the soluble lipase to 6.1 and the optimum temperature remained at 50 ºC after immobilization. The patterns of heat stability indicated that the immobilization process provided the stabilization of the enzyme and the epoxy SiO2-chitosan derivative was almost 30-fold more stable than soluble lipase at 60 ºC. |
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Journal of the Brazilian Chemical Society (Online) |
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Chitosan/siloxane hybrid polymer: synthesis, characterization and performance as a support for immobilizing enzymechitosanhybrid matrixlipaseimmobilizationA hybrid polymer derived from siloxane and chitosan was obtained by sol-gel technique using tetraethoxysilane (TEOS) as a precursor. The hybrid support was chemically modified with epichlorohydrin and used to immobilize lipase from Burkholderia cepacia. The hybrid SiO2-chitosan formed new macromolecular structure in which the inorganic particles are dispersed at the nanometer scale in the organic host matrix and bounding through covalent bonds. A comparative study between free and immobilized lipase was provided in terms of pH, temperature, kinetic parameters and thermal stability. The pH for maximum hydrolysis activity shifted from 7.0 for the soluble lipase to 6.1 and the optimum temperature remained at 50 ºC after immobilization. The patterns of heat stability indicated that the immobilization process provided the stabilization of the enzyme and the epoxy SiO2-chitosan derivative was almost 30-fold more stable than soluble lipase at 60 ºC.Sociedade Brasileira de Química2011-08-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S0103-50532011000800003Journal of the Brazilian Chemical Society v.22 n.8 2011reponame:Journal of the Brazilian Chemical Society (Online)instname:Sociedade Brasileira de Química (SBQ)instacron:SBQ10.1590/S0103-50532011000800003info:eu-repo/semantics/openAccessSilva,Grazielle S.Oliveira,Pedro C.Giordani,Domingos S.Castro,Heizir F. deeng2011-08-04T00:00:00Zoai:scielo:S0103-50532011000800003Revistahttp://jbcs.sbq.org.brONGhttps://old.scielo.br/oai/scielo-oai.php||office@jbcs.sbq.org.br1678-47900103-5053opendoar:2011-08-04T00:00Journal of the Brazilian Chemical Society (Online) - Sociedade Brasileira de Química (SBQ)false |
dc.title.none.fl_str_mv |
Chitosan/siloxane hybrid polymer: synthesis, characterization and performance as a support for immobilizing enzyme |
title |
Chitosan/siloxane hybrid polymer: synthesis, characterization and performance as a support for immobilizing enzyme |
spellingShingle |
Chitosan/siloxane hybrid polymer: synthesis, characterization and performance as a support for immobilizing enzyme Silva,Grazielle S. chitosan hybrid matrix lipase immobilization |
title_short |
Chitosan/siloxane hybrid polymer: synthesis, characterization and performance as a support for immobilizing enzyme |
title_full |
Chitosan/siloxane hybrid polymer: synthesis, characterization and performance as a support for immobilizing enzyme |
title_fullStr |
Chitosan/siloxane hybrid polymer: synthesis, characterization and performance as a support for immobilizing enzyme |
title_full_unstemmed |
Chitosan/siloxane hybrid polymer: synthesis, characterization and performance as a support for immobilizing enzyme |
title_sort |
Chitosan/siloxane hybrid polymer: synthesis, characterization and performance as a support for immobilizing enzyme |
author |
Silva,Grazielle S. |
author_facet |
Silva,Grazielle S. Oliveira,Pedro C. Giordani,Domingos S. Castro,Heizir F. de |
author_role |
author |
author2 |
Oliveira,Pedro C. Giordani,Domingos S. Castro,Heizir F. de |
author2_role |
author author author |
dc.contributor.author.fl_str_mv |
Silva,Grazielle S. Oliveira,Pedro C. Giordani,Domingos S. Castro,Heizir F. de |
dc.subject.por.fl_str_mv |
chitosan hybrid matrix lipase immobilization |
topic |
chitosan hybrid matrix lipase immobilization |
description |
A hybrid polymer derived from siloxane and chitosan was obtained by sol-gel technique using tetraethoxysilane (TEOS) as a precursor. The hybrid support was chemically modified with epichlorohydrin and used to immobilize lipase from Burkholderia cepacia. The hybrid SiO2-chitosan formed new macromolecular structure in which the inorganic particles are dispersed at the nanometer scale in the organic host matrix and bounding through covalent bonds. A comparative study between free and immobilized lipase was provided in terms of pH, temperature, kinetic parameters and thermal stability. The pH for maximum hydrolysis activity shifted from 7.0 for the soluble lipase to 6.1 and the optimum temperature remained at 50 ºC after immobilization. The patterns of heat stability indicated that the immobilization process provided the stabilization of the enzyme and the epoxy SiO2-chitosan derivative was almost 30-fold more stable than soluble lipase at 60 ºC. |
publishDate |
2011 |
dc.date.none.fl_str_mv |
2011-08-01 |
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=S0103-50532011000800003 |
url |
http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0103-50532011000800003 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
10.1590/S0103-50532011000800003 |
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 |
Journal of the Brazilian Chemical Society v.22 n.8 2011 reponame:Journal of the Brazilian Chemical Society (Online) instname:Sociedade Brasileira de Química (SBQ) instacron:SBQ |
instname_str |
Sociedade Brasileira de Química (SBQ) |
instacron_str |
SBQ |
institution |
SBQ |
reponame_str |
Journal of the Brazilian Chemical Society (Online) |
collection |
Journal of the Brazilian Chemical Society (Online) |
repository.name.fl_str_mv |
Journal of the Brazilian Chemical Society (Online) - Sociedade Brasileira de Química (SBQ) |
repository.mail.fl_str_mv |
||office@jbcs.sbq.org.br |
_version_ |
1750318172351758336 |