Immobilization of Lipases Produced by the Endophytic Fungus Cercospora kikuchii on Chitosan Microparticles
Autor(a) principal: | |
---|---|
Data de Publicação: | 2014 |
Outros Autores: | , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Brazilian Archives of Biology and Technology |
Texto Completo: | http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132014000400578 |
Resumo: | This work studied the immobilization of Cercospora kikuchii lipases on chitosan microparticles by chemical attachment on chitosan acetate microparticles activated by glutaraldehyde (CAM) added before or after the enzyme and physical adsorption on highly deacetylated chitosan hydrochloride microparticles (CHM). Lipases covalently immobilized on pre-activated CAM showed better performance retaining 88.4% of the enzymatic activity, with 68.2% of immobilization efficiency (IE). The immobilized enzyme retained an activity of about 53.5 % after five reuses, using p-NPP as substrate. Physical adsorption of lipase onto highly deacetylated CHM showed 46.2 % of enzymatic activity and 28.6% of IE. This immobilized derivative did not lose activity up to 80 days of storage at 4°C, while lipases immobilized on pre-activated CAM maintained its activity up to 180 days at same conditions. Taken together the results indicate that chitosan microparticles provide an optimal microenvironment for the immobilized enzyme to maintain good activity and stability. |
id |
TECPAR-1_2d793519a343b6e3a94dd9e4e55da582 |
---|---|
oai_identifier_str |
oai:scielo:S1516-89132014000400578 |
network_acronym_str |
TECPAR-1 |
network_name_str |
Brazilian Archives of Biology and Technology |
repository_id_str |
|
spelling |
Immobilization of Lipases Produced by the Endophytic Fungus Cercospora kikuchii on Chitosan Microparticlesenzyme immobilizationchitosanCercospora kikuchiilipaseThis work studied the immobilization of Cercospora kikuchii lipases on chitosan microparticles by chemical attachment on chitosan acetate microparticles activated by glutaraldehyde (CAM) added before or after the enzyme and physical adsorption on highly deacetylated chitosan hydrochloride microparticles (CHM). Lipases covalently immobilized on pre-activated CAM showed better performance retaining 88.4% of the enzymatic activity, with 68.2% of immobilization efficiency (IE). The immobilized enzyme retained an activity of about 53.5 % after five reuses, using p-NPP as substrate. Physical adsorption of lipase onto highly deacetylated CHM showed 46.2 % of enzymatic activity and 28.6% of IE. This immobilized derivative did not lose activity up to 80 days of storage at 4°C, while lipases immobilized on pre-activated CAM maintained its activity up to 180 days at same conditions. Taken together the results indicate that chitosan microparticles provide an optimal microenvironment for the immobilized enzyme to maintain good activity and stability.Instituto de Tecnologia do Paraná - Tecpar2014-08-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132014000400578Brazilian Archives of Biology and Technology v.57 n.4 2014reponame:Brazilian Archives of Biology and Technologyinstname:Instituto de Tecnologia do Paraná (Tecpar)instacron:TECPAR10.1590/S1516-8913201402174info:eu-repo/semantics/openAccessCarneiro,Lara Aparecida Buffoni CamposCosta-Silva,Tales AlexandreSouza,Cláudia Regina FernandesBachmann,LucianoOliveira,Wanderley PereiraSaid,Suraiaeng2015-09-03T00:00:00Zoai:scielo:S1516-89132014000400578Revistahttps://www.scielo.br/j/babt/https://old.scielo.br/oai/scielo-oai.phpbabt@tecpar.br||babt@tecpar.br1678-43241516-8913opendoar:2015-09-03T00:00Brazilian Archives of Biology and Technology - Instituto de Tecnologia do Paraná (Tecpar)false |
dc.title.none.fl_str_mv |
Immobilization of Lipases Produced by the Endophytic Fungus Cercospora kikuchii on Chitosan Microparticles |
title |
Immobilization of Lipases Produced by the Endophytic Fungus Cercospora kikuchii on Chitosan Microparticles |
spellingShingle |
Immobilization of Lipases Produced by the Endophytic Fungus Cercospora kikuchii on Chitosan Microparticles Carneiro,Lara Aparecida Buffoni Campos enzyme immobilization chitosan Cercospora kikuchii lipase |
title_short |
Immobilization of Lipases Produced by the Endophytic Fungus Cercospora kikuchii on Chitosan Microparticles |
title_full |
Immobilization of Lipases Produced by the Endophytic Fungus Cercospora kikuchii on Chitosan Microparticles |
title_fullStr |
Immobilization of Lipases Produced by the Endophytic Fungus Cercospora kikuchii on Chitosan Microparticles |
title_full_unstemmed |
Immobilization of Lipases Produced by the Endophytic Fungus Cercospora kikuchii on Chitosan Microparticles |
title_sort |
Immobilization of Lipases Produced by the Endophytic Fungus Cercospora kikuchii on Chitosan Microparticles |
author |
Carneiro,Lara Aparecida Buffoni Campos |
author_facet |
Carneiro,Lara Aparecida Buffoni Campos Costa-Silva,Tales Alexandre Souza,Cláudia Regina Fernandes Bachmann,Luciano Oliveira,Wanderley Pereira Said,Suraia |
author_role |
author |
author2 |
Costa-Silva,Tales Alexandre Souza,Cláudia Regina Fernandes Bachmann,Luciano Oliveira,Wanderley Pereira Said,Suraia |
author2_role |
author author author author author |
dc.contributor.author.fl_str_mv |
Carneiro,Lara Aparecida Buffoni Campos Costa-Silva,Tales Alexandre Souza,Cláudia Regina Fernandes Bachmann,Luciano Oliveira,Wanderley Pereira Said,Suraia |
dc.subject.por.fl_str_mv |
enzyme immobilization chitosan Cercospora kikuchii lipase |
topic |
enzyme immobilization chitosan Cercospora kikuchii lipase |
description |
This work studied the immobilization of Cercospora kikuchii lipases on chitosan microparticles by chemical attachment on chitosan acetate microparticles activated by glutaraldehyde (CAM) added before or after the enzyme and physical adsorption on highly deacetylated chitosan hydrochloride microparticles (CHM). Lipases covalently immobilized on pre-activated CAM showed better performance retaining 88.4% of the enzymatic activity, with 68.2% of immobilization efficiency (IE). The immobilized enzyme retained an activity of about 53.5 % after five reuses, using p-NPP as substrate. Physical adsorption of lipase onto highly deacetylated CHM showed 46.2 % of enzymatic activity and 28.6% of IE. This immobilized derivative did not lose activity up to 80 days of storage at 4°C, while lipases immobilized on pre-activated CAM maintained its activity up to 180 days at same conditions. Taken together the results indicate that chitosan microparticles provide an optimal microenvironment for the immobilized enzyme to maintain good activity and stability. |
publishDate |
2014 |
dc.date.none.fl_str_mv |
2014-08-01 |
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=S1516-89132014000400578 |
url |
http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132014000400578 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
10.1590/S1516-8913201402174 |
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 |
Instituto de Tecnologia do Paraná - Tecpar |
publisher.none.fl_str_mv |
Instituto de Tecnologia do Paraná - Tecpar |
dc.source.none.fl_str_mv |
Brazilian Archives of Biology and Technology v.57 n.4 2014 reponame:Brazilian Archives of Biology and Technology instname:Instituto de Tecnologia do Paraná (Tecpar) instacron:TECPAR |
instname_str |
Instituto de Tecnologia do Paraná (Tecpar) |
instacron_str |
TECPAR |
institution |
TECPAR |
reponame_str |
Brazilian Archives of Biology and Technology |
collection |
Brazilian Archives of Biology and Technology |
repository.name.fl_str_mv |
Brazilian Archives of Biology and Technology - Instituto de Tecnologia do Paraná (Tecpar) |
repository.mail.fl_str_mv |
babt@tecpar.br||babt@tecpar.br |
_version_ |
1750318276431314944 |