Immobilisation of Bacillus subtilis NRC33a levansucrase and some studies on its properties

Detalhes bibliográficos
Autor(a) principal: Esawy,M. A.
Data de Publicação: 2008
Outros Autores: Mahmoud,D. A. R., Fattah,A. F. A.
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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spelling 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
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