Thermal stability of the immobilized fructosyltransferase from Rhodotorula sp

Detalhes bibliográficos
Autor(a) principal: Aguiar-Oliveira,E
Data de Publicação: 2011
Outros Autores: Maugeri,F
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.
id ABEQ-1_5c8b793d46f0a6b028d57abc18a9d399
oai_identifier_str oai:scielo:S0104-66322011000300002
network_acronym_str ABEQ-1
network_name_str Brazilian Journal of Chemical Engineering
repository_id_str
spelling 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

Registros relacionados