Characterization of free and immobilized invertase regarding activity and energy of activation
Invertase from NOVO Nordisk has been immobilized in controlled pore silica particles (diameter: 0.351 mm and mean pore size: 37.5 nm) by covalent binding with the silane-glutaraldehyde method. The activity of the free and immobilized enzyme (IE) was determined with 5% (w/v) sucrose, at 35 to 65ºC and pH from 3 to 7. Maximum activities were found in the pH range from 5 to 6 for free invertase, and pH 4.5 for the IE. Activity yield for the IE was 24%. The Energy of Activation (Ea) was found to be a function of pH, giving for free invertase, Ea = 7.0 and 6.86 kcal/mol at pH 5.0 and 5.5, respectively, whereas for the immobilized enzyme, Ea = 6.55 and 5.93 kcal/mol at pH 4.5 and 5.0, respectively.
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Brazilian Society of Chemical Engineering
2000
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oai:scielo:S0104-663220000004000512001-03-16Characterization of free and immobilized invertase regarding activity and energy of activationBergamasco,R.Bassetti,F.J.Moraes,F.F. deZanin,G.M. invertase immobilized invertase energy of activation sucrose controlled pore silica Invertase from NOVO Nordisk has been immobilized in controlled pore silica particles (diameter: 0.351 mm and mean pore size: 37.5 nm) by covalent binding with the silane-glutaraldehyde method. The activity of the free and immobilized enzyme (IE) was determined with 5% (w/v) sucrose, at 35 to 65ºC and pH from 3 to 7. Maximum activities were found in the pH range from 5 to 6 for free invertase, and pH 4.5 for the IE. Activity yield for the IE was 24%. The Energy of Activation (Ea) was found to be a function of pH, giving for free invertase, Ea = 7.0 and 6.86 kcal/mol at pH 5.0 and 5.5, respectively, whereas for the immobilized enzyme, Ea = 6.55 and 5.93 kcal/mol at pH 4.5 and 5.0, respectively.info:eu-repo/semantics/openAccessBrazilian Society of Chemical EngineeringBrazilian Journal of Chemical Engineering v.17 n.4-7 20002000-12-01info:eu-repo/semantics/articletext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S0104-66322000000400051en10.1590/S0104-66322000000400051 |
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Bergamasco,R. Bassetti,F.J. Moraes,F.F. de Zanin,G.M. |
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Bergamasco,R. Bassetti,F.J. Moraes,F.F. de Zanin,G.M. Characterization of free and immobilized invertase regarding activity and energy of activation |
author_facet |
Bergamasco,R. Bassetti,F.J. Moraes,F.F. de Zanin,G.M. |
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Bergamasco,R. |
title |
Characterization of free and immobilized invertase regarding activity and energy of activation |
title_short |
Characterization of free and immobilized invertase regarding activity and energy of activation |
title_full |
Characterization of free and immobilized invertase regarding activity and energy of activation |
title_fullStr |
Characterization of free and immobilized invertase regarding activity and energy of activation |
title_full_unstemmed |
Characterization of free and immobilized invertase regarding activity and energy of activation |
title_sort |
characterization of free and immobilized invertase regarding activity and energy of activation |
description |
Invertase from NOVO Nordisk has been immobilized in controlled pore silica particles (diameter: 0.351 mm and mean pore size: 37.5 nm) by covalent binding with the silane-glutaraldehyde method. The activity of the free and immobilized enzyme (IE) was determined with 5% (w/v) sucrose, at 35 to 65ºC and pH from 3 to 7. Maximum activities were found in the pH range from 5 to 6 for free invertase, and pH 4.5 for the IE. Activity yield for the IE was 24%. The Energy of Activation (Ea) was found to be a function of pH, giving for free invertase, Ea = 7.0 and 6.86 kcal/mol at pH 5.0 and 5.5, respectively, whereas for the immobilized enzyme, Ea = 6.55 and 5.93 kcal/mol at pH 4.5 and 5.0, respectively. |
publisher |
Brazilian Society of Chemical Engineering |
publishDate |
2000 |
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http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0104-66322000000400051 |
work_keys_str_mv |
AT bergamascor characterizationoffreeandimmobilizedinvertaseregardingactivityandenergyofactivation AT bassettifj characterizationoffreeandimmobilizedinvertaseregardingactivityandenergyofactivation AT moraesffde characterizationoffreeandimmobilizedinvertaseregardingactivityandenergyofactivation AT zaningm characterizationoffreeandimmobilizedinvertaseregardingactivityandenergyofactivation |
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1756411145383575552 |