Evaluation of inorganic matrixes as supports for immobilization of microbial lipase

Detalhes bibliográficos
Autor(a) principal: Castro,H.F.
Data de Publicação: 2000
Outros Autores: Silva,M.L.C.P., Silva,G.L.J.P
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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spelling 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
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