Partitioning optimization of proteins from Zea mays malt in ATPS PEG 6000/CaCl2
Autor(a) principal: | |
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Data de Publicação: | 2007 |
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=S1516-89132007000300020 |
Resumo: | This work aimed to establish the relationship between the compositions and pH of ATPS PEG 6000/CaCl2 and the proteins partition from maize malt and also to simplify the process optimization in ATPS for a statistical model, established by response surface methodology (RSM). Results showed that these were no influence of pH on the phase diagrams and on the composition of tie line length of PEG 6000/CaCl2 ATPS. SRM analyses showed that elevated pH and larger tie line length were the best conditions for recovering of maize malt proteins. The maximum partition coefficient by PEG 6000/CaCl2 ATPS was about 4.2 and was achieved in ATPS in a single purification step. The theoretical maximum partition coefficient was between 4.1-4.3. The process was very suitable for continuous aqueous two-phase purification due to the stability of proteins (e.g. and -amylases) and could increase their content into middle. |
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Brazilian Archives of Biology and Technology |
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Partitioning optimization of proteins from Zea mays malt in ATPS PEG 6000/CaCl2Partitioningoptimizationaqueous two-phase systemsmaize maltPEG 6000CaCl2This work aimed to establish the relationship between the compositions and pH of ATPS PEG 6000/CaCl2 and the proteins partition from maize malt and also to simplify the process optimization in ATPS for a statistical model, established by response surface methodology (RSM). Results showed that these were no influence of pH on the phase diagrams and on the composition of tie line length of PEG 6000/CaCl2 ATPS. SRM analyses showed that elevated pH and larger tie line length were the best conditions for recovering of maize malt proteins. The maximum partition coefficient by PEG 6000/CaCl2 ATPS was about 4.2 and was achieved in ATPS in a single purification step. The theoretical maximum partition coefficient was between 4.1-4.3. The process was very suitable for continuous aqueous two-phase purification due to the stability of proteins (e.g. and -amylases) and could increase their content into middle.Instituto de Tecnologia do Paraná - Tecpar2007-05-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132007000300020Brazilian Archives of Biology and Technology v.50 n.3 2007reponame:Brazilian Archives of Biology and Technologyinstname:Instituto de Tecnologia do Paraná (Tecpar)instacron:TECPAR10.1590/S1516-89132007000300020info:eu-repo/semantics/openAccessFerreira,Graziela BatistaEvangelista,Alex FerreiraSevero Junior,João BaptistaSouza,Roberto Rodrigues deSantana,José Carlos CurveloTambourgi,Elias BasileJordão,Elizabeteeng2007-09-03T00:00:00Zoai:scielo:S1516-89132007000300020Revistahttps://www.scielo.br/j/babt/https://old.scielo.br/oai/scielo-oai.phpbabt@tecpar.br||babt@tecpar.br1678-43241516-8913opendoar:2007-09-03T00:00Brazilian Archives of Biology and Technology - Instituto de Tecnologia do Paraná (Tecpar)false |
dc.title.none.fl_str_mv |
Partitioning optimization of proteins from Zea mays malt in ATPS PEG 6000/CaCl2 |
title |
Partitioning optimization of proteins from Zea mays malt in ATPS PEG 6000/CaCl2 |
spellingShingle |
Partitioning optimization of proteins from Zea mays malt in ATPS PEG 6000/CaCl2 Ferreira,Graziela Batista Partitioning optimization aqueous two-phase systems maize malt PEG 6000 CaCl2 |
title_short |
Partitioning optimization of proteins from Zea mays malt in ATPS PEG 6000/CaCl2 |
title_full |
Partitioning optimization of proteins from Zea mays malt in ATPS PEG 6000/CaCl2 |
title_fullStr |
Partitioning optimization of proteins from Zea mays malt in ATPS PEG 6000/CaCl2 |
title_full_unstemmed |
Partitioning optimization of proteins from Zea mays malt in ATPS PEG 6000/CaCl2 |
title_sort |
Partitioning optimization of proteins from Zea mays malt in ATPS PEG 6000/CaCl2 |
author |
Ferreira,Graziela Batista |
author_facet |
Ferreira,Graziela Batista Evangelista,Alex Ferreira Severo Junior,João Baptista Souza,Roberto Rodrigues de Santana,José Carlos Curvelo Tambourgi,Elias Basile Jordão,Elizabete |
author_role |
author |
author2 |
Evangelista,Alex Ferreira Severo Junior,João Baptista Souza,Roberto Rodrigues de Santana,José Carlos Curvelo Tambourgi,Elias Basile Jordão,Elizabete |
author2_role |
author author author author author author |
dc.contributor.author.fl_str_mv |
Ferreira,Graziela Batista Evangelista,Alex Ferreira Severo Junior,João Baptista Souza,Roberto Rodrigues de Santana,José Carlos Curvelo Tambourgi,Elias Basile Jordão,Elizabete |
dc.subject.por.fl_str_mv |
Partitioning optimization aqueous two-phase systems maize malt PEG 6000 CaCl2 |
topic |
Partitioning optimization aqueous two-phase systems maize malt PEG 6000 CaCl2 |
description |
This work aimed to establish the relationship between the compositions and pH of ATPS PEG 6000/CaCl2 and the proteins partition from maize malt and also to simplify the process optimization in ATPS for a statistical model, established by response surface methodology (RSM). Results showed that these were no influence of pH on the phase diagrams and on the composition of tie line length of PEG 6000/CaCl2 ATPS. SRM analyses showed that elevated pH and larger tie line length were the best conditions for recovering of maize malt proteins. The maximum partition coefficient by PEG 6000/CaCl2 ATPS was about 4.2 and was achieved in ATPS in a single purification step. The theoretical maximum partition coefficient was between 4.1-4.3. The process was very suitable for continuous aqueous two-phase purification due to the stability of proteins (e.g. and -amylases) and could increase their content into middle. |
publishDate |
2007 |
dc.date.none.fl_str_mv |
2007-05-01 |
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=S1516-89132007000300020 |
url |
http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132007000300020 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
10.1590/S1516-89132007000300020 |
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.50 n.3 2007 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_ |
1750318271527124992 |