Penicillium restrictum lipases: A comparative study and characterization of enzymes with different degrees of purity

Detalhes bibliográficos
Autor(a) principal: JESUS,M.F.C.P.
Data de Publicação: 1999
Outros Autores: BRANCO,R.N., SANT'ANNA JR,G.L., FREIRE,D.M.G., SILVA,J.G.
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=S0104-66321999000200002
Resumo: Penicillium restrictum was identified as a promising strain for lipase production due to enzyme production yield and thermal stability of the enzyme. This work presents results of lipase purification and enzyme stability versus pH. Ultrafiltration and precipitation with ammonium sulphate were used as initial purification steps. The partially purified enzyme preparation showed an increase in stability as pH increased. The crude enzymatic preparation was assayed with different oils and tributirin and showed a major catalytic activity for triglycerides of medium/long-chain fatty acids. Further purification steps were conducted on an analytical scale. The initial attempt to use gel filtration was abandoned as lipase lost its stability after this chromatographic procedure. The fast ion-exchange chromatography was performed on a Mono Q column, and two peaks with lipolytic activity were isolated and analysed by electrophoresis.
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spelling Penicillium restrictum lipases: A comparative study and characterization of enzymes with different degrees of puritylipasePenicillium restrictumpurificationcharacterizationstabilityPenicillium restrictum was identified as a promising strain for lipase production due to enzyme production yield and thermal stability of the enzyme. This work presents results of lipase purification and enzyme stability versus pH. Ultrafiltration and precipitation with ammonium sulphate were used as initial purification steps. The partially purified enzyme preparation showed an increase in stability as pH increased. The crude enzymatic preparation was assayed with different oils and tributirin and showed a major catalytic activity for triglycerides of medium/long-chain fatty acids. Further purification steps were conducted on an analytical scale. The initial attempt to use gel filtration was abandoned as lipase lost its stability after this chromatographic procedure. The fast ion-exchange chromatography was performed on a Mono Q column, and two peaks with lipolytic activity were isolated and analysed by electrophoresis.Brazilian Society of Chemical Engineering1999-06-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S0104-66321999000200002Brazilian Journal of Chemical Engineering v.16 n.2 1999reponame:Brazilian Journal of Chemical Engineeringinstname:Associação Brasileira de Engenharia Química (ABEQ)instacron:ABEQ10.1590/S0104-66321999000200002info:eu-repo/semantics/openAccessJESUS,M.F.C.P.BRANCO,R.N.SANT'ANNA JR,G.L.FREIRE,D.M.G.SILVA,J.G.eng1999-09-15T00:00:00Zoai:scielo:S0104-66321999000200002Revistahttps://www.scielo.br/j/bjce/https://old.scielo.br/oai/scielo-oai.phprgiudici@usp.br||rgiudici@usp.br1678-43830104-6632opendoar:1999-09-15T00:00Brazilian Journal of Chemical Engineering - Associação Brasileira de Engenharia Química (ABEQ)false
dc.title.none.fl_str_mv Penicillium restrictum lipases: A comparative study and characterization of enzymes with different degrees of purity
title Penicillium restrictum lipases: A comparative study and characterization of enzymes with different degrees of purity
spellingShingle Penicillium restrictum lipases: A comparative study and characterization of enzymes with different degrees of purity
JESUS,M.F.C.P.
lipase
Penicillium restrictum
purification
characterization
stability
title_short Penicillium restrictum lipases: A comparative study and characterization of enzymes with different degrees of purity
title_full Penicillium restrictum lipases: A comparative study and characterization of enzymes with different degrees of purity
title_fullStr Penicillium restrictum lipases: A comparative study and characterization of enzymes with different degrees of purity
title_full_unstemmed Penicillium restrictum lipases: A comparative study and characterization of enzymes with different degrees of purity
title_sort Penicillium restrictum lipases: A comparative study and characterization of enzymes with different degrees of purity
author JESUS,M.F.C.P.
author_facet JESUS,M.F.C.P.
BRANCO,R.N.
SANT'ANNA JR,G.L.
FREIRE,D.M.G.
SILVA,J.G.
author_role author
author2 BRANCO,R.N.
SANT'ANNA JR,G.L.
FREIRE,D.M.G.
SILVA,J.G.
author2_role author
author
author
author
dc.contributor.author.fl_str_mv JESUS,M.F.C.P.
BRANCO,R.N.
SANT'ANNA JR,G.L.
FREIRE,D.M.G.
SILVA,J.G.
dc.subject.por.fl_str_mv lipase
Penicillium restrictum
purification
characterization
stability
topic lipase
Penicillium restrictum
purification
characterization
stability
description Penicillium restrictum was identified as a promising strain for lipase production due to enzyme production yield and thermal stability of the enzyme. This work presents results of lipase purification and enzyme stability versus pH. Ultrafiltration and precipitation with ammonium sulphate were used as initial purification steps. The partially purified enzyme preparation showed an increase in stability as pH increased. The crude enzymatic preparation was assayed with different oils and tributirin and showed a major catalytic activity for triglycerides of medium/long-chain fatty acids. Further purification steps were conducted on an analytical scale. The initial attempt to use gel filtration was abandoned as lipase lost its stability after this chromatographic procedure. The fast ion-exchange chromatography was performed on a Mono Q column, and two peaks with lipolytic activity were isolated and analysed by electrophoresis.
publishDate 1999
dc.date.none.fl_str_mv 1999-06-01
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=S0104-66321999000200002
url http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0104-66321999000200002
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 10.1590/S0104-66321999000200002
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.16 n.2 1999
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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