Purification and characterisation of an extracellular phytase from Aspergillus niger 11T53A9
Autor(a) principal: | |
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Data de Publicação: | 2009 |
Outros Autores: | , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Brazilian Journal of Microbiology |
Texto Completo: | http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822009000400010 |
Resumo: | An extracellular phytase from Aspergillus niger 11T53A9 was purified about 51-fold to apparent homogeneity with a recovery of 20.3% referred to the phytase activity in the crude extract. Purification was achieved by ammonium sulphate precipitation, ion chromataography and gel filtration. The purified enzyme behaved as a monomeric protein with a molecular mass of about 85 kDa and exhibited maximal phytate-degrading activity at pH 5.0. Optimum temperature for the degradation of phytate was 55°C. The kinetic parameters for the hydrolysis of sodium phytate were determined to be K M = 54 µmol l-1 and k cat = 190 sec-1 at pH 5.0 and 37°C. The purified enzyme was rather specific for phytate dephosphorylation. It was shown that the phytase preferably dephosphorylates myo-inositol hexakisphosphate in a stereospecific way by sequential removal of phosphate groups via D-Ins(1,2,4,5,6)P5, D-Ins(1,2,5,6)P4, D-Ins(1,2,6)P3, D-Ins(1,2)P2 to finally Ins(2)P. |
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Brazilian Journal of Microbiology |
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spelling |
Purification and characterisation of an extracellular phytase from Aspergillus niger 11T53A9Aspergillus nigerphytate-degrading enzymephytatephytaseAn extracellular phytase from Aspergillus niger 11T53A9 was purified about 51-fold to apparent homogeneity with a recovery of 20.3% referred to the phytase activity in the crude extract. Purification was achieved by ammonium sulphate precipitation, ion chromataography and gel filtration. The purified enzyme behaved as a monomeric protein with a molecular mass of about 85 kDa and exhibited maximal phytate-degrading activity at pH 5.0. Optimum temperature for the degradation of phytate was 55°C. The kinetic parameters for the hydrolysis of sodium phytate were determined to be K M = 54 µmol l-1 and k cat = 190 sec-1 at pH 5.0 and 37°C. The purified enzyme was rather specific for phytate dephosphorylation. It was shown that the phytase preferably dephosphorylates myo-inositol hexakisphosphate in a stereospecific way by sequential removal of phosphate groups via D-Ins(1,2,4,5,6)P5, D-Ins(1,2,5,6)P4, D-Ins(1,2,6)P3, D-Ins(1,2)P2 to finally Ins(2)P.Sociedade Brasileira de Microbiologia2009-12-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822009000400010Brazilian Journal of Microbiology v.40 n.4 2009reponame:Brazilian Journal of Microbiologyinstname:Sociedade Brasileira de Microbiologia (SBM)instacron:SBM10.1590/S1517-83822009000400010info:eu-repo/semantics/openAccessGreiner,RalfSilva,Lucineia Gomes daCouri,Soniaeng2009-10-06T00:00:00Zoai:scielo:S1517-83822009000400010Revistahttps://www.scielo.br/j/bjm/ONGhttps://old.scielo.br/oai/scielo-oai.phpbjm@sbmicrobiologia.org.br||mbmartin@usp.br1678-44051517-8382opendoar:2009-10-06T00:00Brazilian Journal of Microbiology - Sociedade Brasileira de Microbiologia (SBM)false |
dc.title.none.fl_str_mv |
Purification and characterisation of an extracellular phytase from Aspergillus niger 11T53A9 |
title |
Purification and characterisation of an extracellular phytase from Aspergillus niger 11T53A9 |
spellingShingle |
Purification and characterisation of an extracellular phytase from Aspergillus niger 11T53A9 Greiner,Ralf Aspergillus niger phytate-degrading enzyme phytate phytase |
title_short |
Purification and characterisation of an extracellular phytase from Aspergillus niger 11T53A9 |
title_full |
Purification and characterisation of an extracellular phytase from Aspergillus niger 11T53A9 |
title_fullStr |
Purification and characterisation of an extracellular phytase from Aspergillus niger 11T53A9 |
title_full_unstemmed |
Purification and characterisation of an extracellular phytase from Aspergillus niger 11T53A9 |
title_sort |
Purification and characterisation of an extracellular phytase from Aspergillus niger 11T53A9 |
author |
Greiner,Ralf |
author_facet |
Greiner,Ralf Silva,Lucineia Gomes da Couri,Sonia |
author_role |
author |
author2 |
Silva,Lucineia Gomes da Couri,Sonia |
author2_role |
author author |
dc.contributor.author.fl_str_mv |
Greiner,Ralf Silva,Lucineia Gomes da Couri,Sonia |
dc.subject.por.fl_str_mv |
Aspergillus niger phytate-degrading enzyme phytate phytase |
topic |
Aspergillus niger phytate-degrading enzyme phytate phytase |
description |
An extracellular phytase from Aspergillus niger 11T53A9 was purified about 51-fold to apparent homogeneity with a recovery of 20.3% referred to the phytase activity in the crude extract. Purification was achieved by ammonium sulphate precipitation, ion chromataography and gel filtration. The purified enzyme behaved as a monomeric protein with a molecular mass of about 85 kDa and exhibited maximal phytate-degrading activity at pH 5.0. Optimum temperature for the degradation of phytate was 55°C. The kinetic parameters for the hydrolysis of sodium phytate were determined to be K M = 54 µmol l-1 and k cat = 190 sec-1 at pH 5.0 and 37°C. The purified enzyme was rather specific for phytate dephosphorylation. It was shown that the phytase preferably dephosphorylates myo-inositol hexakisphosphate in a stereospecific way by sequential removal of phosphate groups via D-Ins(1,2,4,5,6)P5, D-Ins(1,2,5,6)P4, D-Ins(1,2,6)P3, D-Ins(1,2)P2 to finally Ins(2)P. |
publishDate |
2009 |
dc.date.none.fl_str_mv |
2009-12-01 |
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=S1517-83822009000400010 |
url |
http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822009000400010 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
10.1590/S1517-83822009000400010 |
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 |
Sociedade Brasileira de Microbiologia |
publisher.none.fl_str_mv |
Sociedade Brasileira de Microbiologia |
dc.source.none.fl_str_mv |
Brazilian Journal of Microbiology v.40 n.4 2009 reponame:Brazilian Journal of Microbiology instname:Sociedade Brasileira de Microbiologia (SBM) instacron:SBM |
instname_str |
Sociedade Brasileira de Microbiologia (SBM) |
instacron_str |
SBM |
institution |
SBM |
reponame_str |
Brazilian Journal of Microbiology |
collection |
Brazilian Journal of Microbiology |
repository.name.fl_str_mv |
Brazilian Journal of Microbiology - Sociedade Brasileira de Microbiologia (SBM) |
repository.mail.fl_str_mv |
bjm@sbmicrobiologia.org.br||mbmartin@usp.br |
_version_ |
1752122202622263296 |