Penicillium restrictum lipases: A comparative study and characterization of enzymes with different degrees of purity
Autor(a) principal: | |
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Data de Publicação: | 1999 |
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=S0104-66321999000200002 |
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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Brazilian Journal of Chemical Engineering |
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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 |
_version_ |
1754213170391547904 |