Thermal stability and deactivation energy of free and immobilized invertase
Autor(a) principal: | |
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Data de Publicação: | 2000 |
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=S0104-66322000000400050 |
Resumo: | The thermal stability and the energy of deactivation of free invertase and the immobilized enzyme (IE) was measured at temperatures in the range of 35 to 65°C for the hydrolysis of a 5% w/v sucrose solution. The free enzyme at pH 5.0 is stable up to 50°C for a period of 4 h. Invertase immobilized in controlled pore silica by the silane-glutaraldehyde covalent method is stable up to 55ºC, in pH 4.5 for the same period. For higher temperatures the enzyme deactivation follows the exponential decay model and half-lives are 0.53, 1.80, and 13.9 h for free invertase, at 65, 60, and 55ºC, respectively. For the IE half-lives are 0.48, 1.83, and 20.9 h, at 65, 60, and 55ºC, respectively. The IE is more stable than the free invertase; the energy of deactivation being 83.1 kcal/mol for the IE and 72.0 kcal/mol for the free enzyme. |
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Brazilian Journal of Chemical Engineering |
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Thermal stability and deactivation energy of free and immobilized invertaseinvertasethermal stabilityimmobilized invertasesucroseenergy of deactivationThe thermal stability and the energy of deactivation of free invertase and the immobilized enzyme (IE) was measured at temperatures in the range of 35 to 65°C for the hydrolysis of a 5% w/v sucrose solution. The free enzyme at pH 5.0 is stable up to 50°C for a period of 4 h. Invertase immobilized in controlled pore silica by the silane-glutaraldehyde covalent method is stable up to 55ºC, in pH 4.5 for the same period. For higher temperatures the enzyme deactivation follows the exponential decay model and half-lives are 0.53, 1.80, and 13.9 h for free invertase, at 65, 60, and 55ºC, respectively. For the IE half-lives are 0.48, 1.83, and 20.9 h, at 65, 60, and 55ºC, respectively. The IE is more stable than the free invertase; the energy of deactivation being 83.1 kcal/mol for the IE and 72.0 kcal/mol for the free enzyme.Brazilian Society of Chemical Engineering2000-12-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S0104-66322000000400050Brazilian Journal of Chemical Engineering v.17 n.4-7 2000reponame:Brazilian Journal of Chemical Engineeringinstname:Associação Brasileira de Engenharia Química (ABEQ)instacron:ABEQ10.1590/S0104-66322000000400050info:eu-repo/semantics/openAccessBassetti,F.J.Bergamasco,R.Moraes,F.F.Zanin,G.M.eng2001-03-16T00:00:00Zoai:scielo:S0104-66322000000400050Revistahttps://www.scielo.br/j/bjce/https://old.scielo.br/oai/scielo-oai.phprgiudici@usp.br||rgiudici@usp.br1678-43830104-6632opendoar:2001-03-16T00:00Brazilian Journal of Chemical Engineering - Associação Brasileira de Engenharia Química (ABEQ)false |
dc.title.none.fl_str_mv |
Thermal stability and deactivation energy of free and immobilized invertase |
title |
Thermal stability and deactivation energy of free and immobilized invertase |
spellingShingle |
Thermal stability and deactivation energy of free and immobilized invertase Bassetti,F.J. invertase thermal stability immobilized invertase sucrose energy of deactivation |
title_short |
Thermal stability and deactivation energy of free and immobilized invertase |
title_full |
Thermal stability and deactivation energy of free and immobilized invertase |
title_fullStr |
Thermal stability and deactivation energy of free and immobilized invertase |
title_full_unstemmed |
Thermal stability and deactivation energy of free and immobilized invertase |
title_sort |
Thermal stability and deactivation energy of free and immobilized invertase |
author |
Bassetti,F.J. |
author_facet |
Bassetti,F.J. Bergamasco,R. Moraes,F.F. Zanin,G.M. |
author_role |
author |
author2 |
Bergamasco,R. Moraes,F.F. Zanin,G.M. |
author2_role |
author author author |
dc.contributor.author.fl_str_mv |
Bassetti,F.J. Bergamasco,R. Moraes,F.F. Zanin,G.M. |
dc.subject.por.fl_str_mv |
invertase thermal stability immobilized invertase sucrose energy of deactivation |
topic |
invertase thermal stability immobilized invertase sucrose energy of deactivation |
description |
The thermal stability and the energy of deactivation of free invertase and the immobilized enzyme (IE) was measured at temperatures in the range of 35 to 65°C for the hydrolysis of a 5% w/v sucrose solution. The free enzyme at pH 5.0 is stable up to 50°C for a period of 4 h. Invertase immobilized in controlled pore silica by the silane-glutaraldehyde covalent method is stable up to 55ºC, in pH 4.5 for the same period. For higher temperatures the enzyme deactivation follows the exponential decay model and half-lives are 0.53, 1.80, and 13.9 h for free invertase, at 65, 60, and 55ºC, respectively. For the IE half-lives are 0.48, 1.83, and 20.9 h, at 65, 60, and 55ºC, respectively. The IE is more stable than the free invertase; the energy of deactivation being 83.1 kcal/mol for the IE and 72.0 kcal/mol for the free enzyme. |
publishDate |
2000 |
dc.date.none.fl_str_mv |
2000-12-01 |
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=S0104-66322000000400050 |
url |
http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0104-66322000000400050 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
10.1590/S0104-66322000000400050 |
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.17 n.4-7 2000 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_ |
1754213170791055360 |