Thermal stability of the immobilized fructosyltransferase from Rhodotorula sp
Autor(a) principal: | |
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Data de Publicação: | 2011 |
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=S0104-66322011000300002 |
Resumo: | The thermal stability of the extracellular fructosyltransferase (FTase) from Rhodotorula sp., recovered from cultivation medium by ethanol precipitation and immobilized onto niobium ore, was studied by Arrhenius plot, half - life profile, half - inactivation temperature (T50) and thermodynamic parameters. The Arrhenius plot showed two different behaviors with different deactivation energies (Ead) only after immobilization, the transition occurring in the temperature interval between 51 and 52ºC. T50 for the free enzyme was estimated to be around 62ºC and, after immobilization, 66ºC. After 15 minutes at 52ºC, it was also possible to observe enzymatic activation for both the free and immobilized forms, but greater activation was achieved at pH 4.5 with the immobilized enzyme. Between 47 - 51ºC the immobilized enzyme was more stable than the free enzyme, with pH 6.0 being the more stable condition for the immobilized enzyme. However, above 52ºC the free form was more stable. |
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Brazilian Journal of Chemical Engineering |
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|
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Thermal stability of the immobilized fructosyltransferase from Rhodotorula spNiobiumAdsorptionHalf-lifeThermal activationArrhenius plotDimerThe thermal stability of the extracellular fructosyltransferase (FTase) from Rhodotorula sp., recovered from cultivation medium by ethanol precipitation and immobilized onto niobium ore, was studied by Arrhenius plot, half - life profile, half - inactivation temperature (T50) and thermodynamic parameters. The Arrhenius plot showed two different behaviors with different deactivation energies (Ead) only after immobilization, the transition occurring in the temperature interval between 51 and 52ºC. T50 for the free enzyme was estimated to be around 62ºC and, after immobilization, 66ºC. After 15 minutes at 52ºC, it was also possible to observe enzymatic activation for both the free and immobilized forms, but greater activation was achieved at pH 4.5 with the immobilized enzyme. Between 47 - 51ºC the immobilized enzyme was more stable than the free enzyme, with pH 6.0 being the more stable condition for the immobilized enzyme. However, above 52ºC the free form was more stable.Brazilian Society of Chemical Engineering2011-09-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S0104-66322011000300002Brazilian Journal of Chemical Engineering v.28 n.3 2011reponame:Brazilian Journal of Chemical Engineeringinstname:Associação Brasileira de Engenharia Química (ABEQ)instacron:ABEQ10.1590/S0104-66322011000300002info:eu-repo/semantics/openAccessAguiar-Oliveira,EMaugeri,Feng2011-09-01T00:00:00Zoai:scielo:S0104-66322011000300002Revistahttps://www.scielo.br/j/bjce/https://old.scielo.br/oai/scielo-oai.phprgiudici@usp.br||rgiudici@usp.br1678-43830104-6632opendoar:2011-09-01T00:00Brazilian Journal of Chemical Engineering - Associação Brasileira de Engenharia Química (ABEQ)false |
dc.title.none.fl_str_mv |
Thermal stability of the immobilized fructosyltransferase from Rhodotorula sp |
title |
Thermal stability of the immobilized fructosyltransferase from Rhodotorula sp |
spellingShingle |
Thermal stability of the immobilized fructosyltransferase from Rhodotorula sp Aguiar-Oliveira,E Niobium Adsorption Half-life Thermal activation Arrhenius plot Dimer |
title_short |
Thermal stability of the immobilized fructosyltransferase from Rhodotorula sp |
title_full |
Thermal stability of the immobilized fructosyltransferase from Rhodotorula sp |
title_fullStr |
Thermal stability of the immobilized fructosyltransferase from Rhodotorula sp |
title_full_unstemmed |
Thermal stability of the immobilized fructosyltransferase from Rhodotorula sp |
title_sort |
Thermal stability of the immobilized fructosyltransferase from Rhodotorula sp |
author |
Aguiar-Oliveira,E |
author_facet |
Aguiar-Oliveira,E Maugeri,F |
author_role |
author |
author2 |
Maugeri,F |
author2_role |
author |
dc.contributor.author.fl_str_mv |
Aguiar-Oliveira,E Maugeri,F |
dc.subject.por.fl_str_mv |
Niobium Adsorption Half-life Thermal activation Arrhenius plot Dimer |
topic |
Niobium Adsorption Half-life Thermal activation Arrhenius plot Dimer |
description |
The thermal stability of the extracellular fructosyltransferase (FTase) from Rhodotorula sp., recovered from cultivation medium by ethanol precipitation and immobilized onto niobium ore, was studied by Arrhenius plot, half - life profile, half - inactivation temperature (T50) and thermodynamic parameters. The Arrhenius plot showed two different behaviors with different deactivation energies (Ead) only after immobilization, the transition occurring in the temperature interval between 51 and 52ºC. T50 for the free enzyme was estimated to be around 62ºC and, after immobilization, 66ºC. After 15 minutes at 52ºC, it was also possible to observe enzymatic activation for both the free and immobilized forms, but greater activation was achieved at pH 4.5 with the immobilized enzyme. Between 47 - 51ºC the immobilized enzyme was more stable than the free enzyme, with pH 6.0 being the more stable condition for the immobilized enzyme. However, above 52ºC the free form was more stable. |
publishDate |
2011 |
dc.date.none.fl_str_mv |
2011-09-01 |
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=S0104-66322011000300002 |
url |
http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0104-66322011000300002 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
10.1590/S0104-66322011000300002 |
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.28 n.3 2011 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_ |
1754213173469118464 |