Immobilisation of Bacillus subtilis NRC33a levansucrase and some studies on its properties
Autor(a) principal: | |
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Data de Publicação: | 2008 |
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=S0104-66322008000200003 |
Resumo: | Bacillus subtilis NRC33a levansucrase was immobilised on different carriers using different immobilisation methods including physical adsorption, covalent binding, ionic binding and entrapment. The immobilised enzyme prepared by covalent binding on chitosan through 3% gluteraldehyde had the highest immobilization yield (81.51%). Therefore, it was used as a typical example for Bacillus subtilis NRC33a immobilised levansucrase and its properties were investigated. The time of the reaction and substrate concentration revealed that the activity of the immobilised enzyme was relatively lower than the free enzyme. The immobilised levansucrase showed a slight increase in activity compared with the free enzyme above 35°C. The activation energies were 6.62 and 9.27 kcal mol-1 for free and immobilised enzyme respectively. Although the thermal stability of the immobilised levansucrase was significantly improved in comparison to the free form, the deactivation energy of the immobilised enzyme was lower than that of the free enzyme. The half life of the immobilised and free levansucrase was also determined. The effect of different pH values reported that at acidic pH the activity of the immobilised levansucrase was higher than that of the free enzyme. The study of pH stability of free and immobilised levansucrase showed that the immobilisation process protected the enzyme from alkaline and severe acidic media. The effect of various metal ions showed that the free levansucrase was more sensitive to the inhibitory effect of the investigated substances. Immobilised levansucrase retained 51.13% after 14 repeated uses. |
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Brazilian Journal of Chemical Engineering |
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Immobilisation of Bacillus subtilis NRC33a levansucrase and some studies on its propertiesImmobilisationBacillus subtilisLevansucraseFructooligosaccharidesBacillus subtilis NRC33a levansucrase was immobilised on different carriers using different immobilisation methods including physical adsorption, covalent binding, ionic binding and entrapment. The immobilised enzyme prepared by covalent binding on chitosan through 3% gluteraldehyde had the highest immobilization yield (81.51%). Therefore, it was used as a typical example for Bacillus subtilis NRC33a immobilised levansucrase and its properties were investigated. The time of the reaction and substrate concentration revealed that the activity of the immobilised enzyme was relatively lower than the free enzyme. The immobilised levansucrase showed a slight increase in activity compared with the free enzyme above 35°C. The activation energies were 6.62 and 9.27 kcal mol-1 for free and immobilised enzyme respectively. Although the thermal stability of the immobilised levansucrase was significantly improved in comparison to the free form, the deactivation energy of the immobilised enzyme was lower than that of the free enzyme. The half life of the immobilised and free levansucrase was also determined. The effect of different pH values reported that at acidic pH the activity of the immobilised levansucrase was higher than that of the free enzyme. The study of pH stability of free and immobilised levansucrase showed that the immobilisation process protected the enzyme from alkaline and severe acidic media. The effect of various metal ions showed that the free levansucrase was more sensitive to the inhibitory effect of the investigated substances. Immobilised levansucrase retained 51.13% after 14 repeated uses.Brazilian Society of Chemical Engineering2008-06-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S0104-66322008000200003Brazilian Journal of Chemical Engineering v.25 n.2 2008reponame:Brazilian Journal of Chemical Engineeringinstname:Associação Brasileira de Engenharia Química (ABEQ)instacron:ABEQ10.1590/S0104-66322008000200003info:eu-repo/semantics/openAccessEsawy,M. A.Mahmoud,D. A. R.Fattah,A. F. A.eng2008-07-03T00:00:00Zoai:scielo:S0104-66322008000200003Revistahttps://www.scielo.br/j/bjce/https://old.scielo.br/oai/scielo-oai.phprgiudici@usp.br||rgiudici@usp.br1678-43830104-6632opendoar:2008-07-03T00:00Brazilian Journal of Chemical Engineering - Associação Brasileira de Engenharia Química (ABEQ)false |
dc.title.none.fl_str_mv |
Immobilisation of Bacillus subtilis NRC33a levansucrase and some studies on its properties |
title |
Immobilisation of Bacillus subtilis NRC33a levansucrase and some studies on its properties |
spellingShingle |
Immobilisation of Bacillus subtilis NRC33a levansucrase and some studies on its properties Esawy,M. A. Immobilisation Bacillus subtilis Levansucrase Fructooligosaccharides |
title_short |
Immobilisation of Bacillus subtilis NRC33a levansucrase and some studies on its properties |
title_full |
Immobilisation of Bacillus subtilis NRC33a levansucrase and some studies on its properties |
title_fullStr |
Immobilisation of Bacillus subtilis NRC33a levansucrase and some studies on its properties |
title_full_unstemmed |
Immobilisation of Bacillus subtilis NRC33a levansucrase and some studies on its properties |
title_sort |
Immobilisation of Bacillus subtilis NRC33a levansucrase and some studies on its properties |
author |
Esawy,M. A. |
author_facet |
Esawy,M. A. Mahmoud,D. A. R. Fattah,A. F. A. |
author_role |
author |
author2 |
Mahmoud,D. A. R. Fattah,A. F. A. |
author2_role |
author author |
dc.contributor.author.fl_str_mv |
Esawy,M. A. Mahmoud,D. A. R. Fattah,A. F. A. |
dc.subject.por.fl_str_mv |
Immobilisation Bacillus subtilis Levansucrase Fructooligosaccharides |
topic |
Immobilisation Bacillus subtilis Levansucrase Fructooligosaccharides |
description |
Bacillus subtilis NRC33a levansucrase was immobilised on different carriers using different immobilisation methods including physical adsorption, covalent binding, ionic binding and entrapment. The immobilised enzyme prepared by covalent binding on chitosan through 3% gluteraldehyde had the highest immobilization yield (81.51%). Therefore, it was used as a typical example for Bacillus subtilis NRC33a immobilised levansucrase and its properties were investigated. The time of the reaction and substrate concentration revealed that the activity of the immobilised enzyme was relatively lower than the free enzyme. The immobilised levansucrase showed a slight increase in activity compared with the free enzyme above 35°C. The activation energies were 6.62 and 9.27 kcal mol-1 for free and immobilised enzyme respectively. Although the thermal stability of the immobilised levansucrase was significantly improved in comparison to the free form, the deactivation energy of the immobilised enzyme was lower than that of the free enzyme. The half life of the immobilised and free levansucrase was also determined. The effect of different pH values reported that at acidic pH the activity of the immobilised levansucrase was higher than that of the free enzyme. The study of pH stability of free and immobilised levansucrase showed that the immobilisation process protected the enzyme from alkaline and severe acidic media. The effect of various metal ions showed that the free levansucrase was more sensitive to the inhibitory effect of the investigated substances. Immobilised levansucrase retained 51.13% after 14 repeated uses. |
publishDate |
2008 |
dc.date.none.fl_str_mv |
2008-06-01 |
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=S0104-66322008000200003 |
url |
http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0104-66322008000200003 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
10.1590/S0104-66322008000200003 |
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.25 n.2 2008 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_ |
1754213172636549120 |