Evaluation of inorganic matrixes as supports for immobilization of microbial lipase
Autor(a) principal: | |
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Data de Publicação: | 2000 |
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=S0104-66322000000400048 |
Resumo: | Candida rugosa was immobilized by physical adsorption on several inorganic supports using hexane as coupling medium. The enzymatic activities of the different derivatives were determined by both hydrolysis of olive oil and esterification of n-butanol with butyric acid. The results were compared to previous data obtained by using a controlled porous silica matrix. The goal was to contribute in searching inexpensive supports for optimum lipase performance. All supports examined exhibited good properties for binding the enzyme lipase. Zirconium phosphate was the best support, giving the highest percentage of protein fixation (86%) and the highest retention of lipase activity after immobilization (34%). The operational stability performance for niobium oxide derivative was improved by previously activated the support with silane and glutaraldehyde. Thermal stabilities were also examined by thermal gravimetric analysis (TG). |
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Brazilian Journal of Chemical Engineering |
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Evaluation of inorganic matrixes as supports for immobilization of microbial lipaseInorganic matrixeslipaseimmobilizationesterificationoperational stabilitythermal stabilityCandida rugosa was immobilized by physical adsorption on several inorganic supports using hexane as coupling medium. The enzymatic activities of the different derivatives were determined by both hydrolysis of olive oil and esterification of n-butanol with butyric acid. The results were compared to previous data obtained by using a controlled porous silica matrix. The goal was to contribute in searching inexpensive supports for optimum lipase performance. All supports examined exhibited good properties for binding the enzyme lipase. Zirconium phosphate was the best support, giving the highest percentage of protein fixation (86%) and the highest retention of lipase activity after immobilization (34%). The operational stability performance for niobium oxide derivative was improved by previously activated the support with silane and glutaraldehyde. Thermal stabilities were also examined by thermal gravimetric analysis (TG).Brazilian Society of Chemical Engineering2000-12-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S0104-66322000000400048Brazilian Journal of Chemical Engineering v.17 n.4-7 2000reponame:Brazilian Journal of Chemical Engineeringinstname:Associação Brasileira de Engenharia Química (ABEQ)instacron:ABEQ10.1590/S0104-66322000000400048info:eu-repo/semantics/openAccessCastro,H.F.Silva,M.L.C.P.Silva,G.L.J.Peng2001-03-16T00:00:00Zoai:scielo:S0104-66322000000400048Revistahttps://www.scielo.br/j/bjce/https://old.scielo.br/oai/scielo-oai.phprgiudici@usp.br||rgiudici@usp.br1678-43830104-6632opendoar:2001-03-16T00:00Brazilian Journal of Chemical Engineering - Associação Brasileira de Engenharia Química (ABEQ)false |
dc.title.none.fl_str_mv |
Evaluation of inorganic matrixes as supports for immobilization of microbial lipase |
title |
Evaluation of inorganic matrixes as supports for immobilization of microbial lipase |
spellingShingle |
Evaluation of inorganic matrixes as supports for immobilization of microbial lipase Castro,H.F. Inorganic matrixes lipase immobilization esterification operational stability thermal stability |
title_short |
Evaluation of inorganic matrixes as supports for immobilization of microbial lipase |
title_full |
Evaluation of inorganic matrixes as supports for immobilization of microbial lipase |
title_fullStr |
Evaluation of inorganic matrixes as supports for immobilization of microbial lipase |
title_full_unstemmed |
Evaluation of inorganic matrixes as supports for immobilization of microbial lipase |
title_sort |
Evaluation of inorganic matrixes as supports for immobilization of microbial lipase |
author |
Castro,H.F. |
author_facet |
Castro,H.F. Silva,M.L.C.P. Silva,G.L.J.P |
author_role |
author |
author2 |
Silva,M.L.C.P. Silva,G.L.J.P |
author2_role |
author author |
dc.contributor.author.fl_str_mv |
Castro,H.F. Silva,M.L.C.P. Silva,G.L.J.P |
dc.subject.por.fl_str_mv |
Inorganic matrixes lipase immobilization esterification operational stability thermal stability |
topic |
Inorganic matrixes lipase immobilization esterification operational stability thermal stability |
description |
Candida rugosa was immobilized by physical adsorption on several inorganic supports using hexane as coupling medium. The enzymatic activities of the different derivatives were determined by both hydrolysis of olive oil and esterification of n-butanol with butyric acid. The results were compared to previous data obtained by using a controlled porous silica matrix. The goal was to contribute in searching inexpensive supports for optimum lipase performance. All supports examined exhibited good properties for binding the enzyme lipase. Zirconium phosphate was the best support, giving the highest percentage of protein fixation (86%) and the highest retention of lipase activity after immobilization (34%). The operational stability performance for niobium oxide derivative was improved by previously activated the support with silane and glutaraldehyde. Thermal stabilities were also examined by thermal gravimetric analysis (TG). |
publishDate |
2000 |
dc.date.none.fl_str_mv |
2000-12-01 |
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=S0104-66322000000400048 |
url |
http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0104-66322000000400048 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
10.1590/S0104-66322000000400048 |
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.17 n.4-7 2000 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_ |
1754213170787909632 |