Biochemical characterisation of a glucoamylase from Aspergillus niger produced by solid-state fermentation
Autor(a) principal: | |
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Data de Publicação: | 2011 |
Outros Autores: | , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Brazilian Archives of Biology and Technology |
Texto Completo: | http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132011000300018 |
Resumo: | In this work, glucoamylase was produced by Aspergillus niger in solid-state fermentation. The enzyme was partially purified by ammonium sulphate precipitation and ion exchange and gel filtration chromatographies. Its molecular mass was estimated as 118.17 kDa by electrophoresis. The partially purified enzyme had an optimum pH range of 4.5-5.0 and an optimum temperature of 60 °C, with average activity 152.85 U mL-1. Thermal and pH stability assays with the crude extract showed that more than 60 % of the activity remained at pH 4.6 and 60 °C, even after an exposition to these conditions longer than 24 h. Yet, after purification, the enzyme was stable at these for at least 4 h, which indicated that its purification for use in starch saccharification was inadvisable. K M and Vmax were 0.34 mg mL-1 and 160.22 U mL-1, respectively. |
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Biochemical characterisation of a glucoamylase from Aspergillus niger produced by solid-state fermentationglucoamylaseAspergillus nigersolid-state fermentationbiochemical characterizationpurificationIn this work, glucoamylase was produced by Aspergillus niger in solid-state fermentation. The enzyme was partially purified by ammonium sulphate precipitation and ion exchange and gel filtration chromatographies. Its molecular mass was estimated as 118.17 kDa by electrophoresis. The partially purified enzyme had an optimum pH range of 4.5-5.0 and an optimum temperature of 60 °C, with average activity 152.85 U mL-1. Thermal and pH stability assays with the crude extract showed that more than 60 % of the activity remained at pH 4.6 and 60 °C, even after an exposition to these conditions longer than 24 h. Yet, after purification, the enzyme was stable at these for at least 4 h, which indicated that its purification for use in starch saccharification was inadvisable. K M and Vmax were 0.34 mg mL-1 and 160.22 U mL-1, respectively.Instituto de Tecnologia do Paraná - Tecpar2011-06-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132011000300018Brazilian Archives of Biology and Technology v.54 n.3 2011reponame:Brazilian Archives of Biology and Technologyinstname:Instituto de Tecnologia do Paraná (Tecpar)instacron:TECPAR10.1590/S1516-89132011000300018info:eu-repo/semantics/openAccessSlivinski,Christiane TrevisanMachado,Alex Vinicius LopesIulek,JorgeAyub,Ricardo AntônioAlmeida,Mareci Mendes deeng2011-06-13T00:00:00Zoai:scielo:S1516-89132011000300018Revistahttps://www.scielo.br/j/babt/https://old.scielo.br/oai/scielo-oai.phpbabt@tecpar.br||babt@tecpar.br1678-43241516-8913opendoar:2011-06-13T00:00Brazilian Archives of Biology and Technology - Instituto de Tecnologia do Paraná (Tecpar)false |
dc.title.none.fl_str_mv |
Biochemical characterisation of a glucoamylase from Aspergillus niger produced by solid-state fermentation |
title |
Biochemical characterisation of a glucoamylase from Aspergillus niger produced by solid-state fermentation |
spellingShingle |
Biochemical characterisation of a glucoamylase from Aspergillus niger produced by solid-state fermentation Slivinski,Christiane Trevisan glucoamylase Aspergillus niger solid-state fermentation biochemical characterization purification |
title_short |
Biochemical characterisation of a glucoamylase from Aspergillus niger produced by solid-state fermentation |
title_full |
Biochemical characterisation of a glucoamylase from Aspergillus niger produced by solid-state fermentation |
title_fullStr |
Biochemical characterisation of a glucoamylase from Aspergillus niger produced by solid-state fermentation |
title_full_unstemmed |
Biochemical characterisation of a glucoamylase from Aspergillus niger produced by solid-state fermentation |
title_sort |
Biochemical characterisation of a glucoamylase from Aspergillus niger produced by solid-state fermentation |
author |
Slivinski,Christiane Trevisan |
author_facet |
Slivinski,Christiane Trevisan Machado,Alex Vinicius Lopes Iulek,Jorge Ayub,Ricardo Antônio Almeida,Mareci Mendes de |
author_role |
author |
author2 |
Machado,Alex Vinicius Lopes Iulek,Jorge Ayub,Ricardo Antônio Almeida,Mareci Mendes de |
author2_role |
author author author author |
dc.contributor.author.fl_str_mv |
Slivinski,Christiane Trevisan Machado,Alex Vinicius Lopes Iulek,Jorge Ayub,Ricardo Antônio Almeida,Mareci Mendes de |
dc.subject.por.fl_str_mv |
glucoamylase Aspergillus niger solid-state fermentation biochemical characterization purification |
topic |
glucoamylase Aspergillus niger solid-state fermentation biochemical characterization purification |
description |
In this work, glucoamylase was produced by Aspergillus niger in solid-state fermentation. The enzyme was partially purified by ammonium sulphate precipitation and ion exchange and gel filtration chromatographies. Its molecular mass was estimated as 118.17 kDa by electrophoresis. The partially purified enzyme had an optimum pH range of 4.5-5.0 and an optimum temperature of 60 °C, with average activity 152.85 U mL-1. Thermal and pH stability assays with the crude extract showed that more than 60 % of the activity remained at pH 4.6 and 60 °C, even after an exposition to these conditions longer than 24 h. Yet, after purification, the enzyme was stable at these for at least 4 h, which indicated that its purification for use in starch saccharification was inadvisable. K M and Vmax were 0.34 mg mL-1 and 160.22 U mL-1, respectively. |
publishDate |
2011 |
dc.date.none.fl_str_mv |
2011-06-01 |
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=S1516-89132011000300018 |
url |
http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132011000300018 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
10.1590/S1516-89132011000300018 |
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 |
Instituto de Tecnologia do Paraná - Tecpar |
publisher.none.fl_str_mv |
Instituto de Tecnologia do Paraná - Tecpar |
dc.source.none.fl_str_mv |
Brazilian Archives of Biology and Technology v.54 n.3 2011 reponame:Brazilian Archives of Biology and Technology instname:Instituto de Tecnologia do Paraná (Tecpar) instacron:TECPAR |
instname_str |
Instituto de Tecnologia do Paraná (Tecpar) |
instacron_str |
TECPAR |
institution |
TECPAR |
reponame_str |
Brazilian Archives of Biology and Technology |
collection |
Brazilian Archives of Biology and Technology |
repository.name.fl_str_mv |
Brazilian Archives of Biology and Technology - Instituto de Tecnologia do Paraná (Tecpar) |
repository.mail.fl_str_mv |
babt@tecpar.br||babt@tecpar.br |
_version_ |
1750318274508226560 |