Immobilization of glucosyltransferase from Erwinia sp. using two different techniques

Autores
Contesini, Fabiano Jares; Ibarguren, Carolina; Grosso, Carlos Raimundo Ferreira; de Oliveira Carvalho, Patrícia; Sato, Hélia Harumi
Año de publicación
2012
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Two different techniques of glucosyltransferase immobilization were studied for the conversion of sucrose into isomaltulose. The optimum conditions for immobilization of Erwinia sp. glucosyltransferase onto Celite 545, determined using response surface methodology, was pH 4.0 and 170. U. of. glucosyltransferase/g of Celite 545. Using this conditions more than 60% conversion of sucrose into isomaltulose can be obtained. The immobilization of glucosyltransferase was also studied by its entrapment in microcapsules of low-methoxyl pectin and fat (butter and oleic acid). The non-lyophilized microcapsules of pectin, containing the enzyme and fat, showed higher glucosyltransferase activity, compared with lyophilized microcapsules containing enzyme plus fat, and also lyophilized microcapsules containing enzyme without fat addition. The non-lyophilized microcapsules of pectin containing the glucosyltransferase and fat, converted 30% of sucrose into isomaltulose in the first batch. However the conversion decreased to 5% at the 10th batch, indicating inactivation of the enzyme. © 2012 Elsevier B.V.
Fil: Contesini, Fabiano Jares. Universidade Estadual de Campinas; Brasil
Fil: Ibarguren, Carolina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Salta. Instituto de Investigaciones para la Industria Química. Universidad Nacional de Salta. Facultad de Ingeniería. Instituto de Investigaciones para la Industria Química; Argentina
Fil: Grosso, Carlos Raimundo Ferreira. Universidade Estadual de Campinas; Brasil
Fil: de Oliveira Carvalho, Patrícia. University São Francisco; Brasil
Fil: Sato, Hélia Harumi. Universidade Estadual de Campinas; Brasil
Materia
Erwinia Sp.
Glucosyltransferase
Immobilization
Isomaltulose
Trehalulose
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/60948
Acceder
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network_acronym_str CONICETDig
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network_name_str CONICET Digital (CONICET)
spelling Immobilization of glucosyltransferase from Erwinia sp. using two different techniquesContesini, Fabiano JaresIbarguren, CarolinaGrosso, Carlos Raimundo Ferreirade Oliveira Carvalho, PatríciaSato, Hélia HarumiErwinia Sp.GlucosyltransferaseImmobilizationIsomaltuloseTrehalulosehttps://purl.org/becyt/ford/2.9https://purl.org/becyt/ford/2Two different techniques of glucosyltransferase immobilization were studied for the conversion of sucrose into isomaltulose. The optimum conditions for immobilization of Erwinia sp. glucosyltransferase onto Celite 545, determined using response surface methodology, was pH 4.0 and 170. U. of. glucosyltransferase/g of Celite 545. Using this conditions more than 60% conversion of sucrose into isomaltulose can be obtained. The immobilization of glucosyltransferase was also studied by its entrapment in microcapsules of low-methoxyl pectin and fat (butter and oleic acid). The non-lyophilized microcapsules of pectin, containing the enzyme and fat, showed higher glucosyltransferase activity, compared with lyophilized microcapsules containing enzyme plus fat, and also lyophilized microcapsules containing enzyme without fat addition. The non-lyophilized microcapsules of pectin containing the glucosyltransferase and fat, converted 30% of sucrose into isomaltulose in the first batch. However the conversion decreased to 5% at the 10th batch, indicating inactivation of the enzyme. © 2012 Elsevier B.V.Fil: Contesini, Fabiano Jares. Universidade Estadual de Campinas; BrasilFil: Ibarguren, Carolina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Salta. Instituto de Investigaciones para la Industria Química. Universidad Nacional de Salta. Facultad de Ingeniería. Instituto de Investigaciones para la Industria Química; ArgentinaFil: Grosso, Carlos Raimundo Ferreira. Universidade Estadual de Campinas; BrasilFil: de Oliveira Carvalho, Patrícia. University São Francisco; BrasilFil: Sato, Hélia Harumi. Universidade Estadual de Campinas; BrasilElsevier Science2012-04info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/60948Contesini, Fabiano Jares; Ibarguren, Carolina; Grosso, Carlos Raimundo Ferreira; de Oliveira Carvalho, Patrícia; Sato, Hélia Harumi; Immobilization of glucosyltransferase from Erwinia sp. using two different techniques; Elsevier Science; Journal of Biotechnology; 158; 3; 4-2012; 137-1430168-1656CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1016/j.jbiotec.2012.01.012info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S016816561200034Xinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T09:59:07Zoai:ri.conicet.gov.ar:11336/60948instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-03 09:59:08.151CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Immobilization of glucosyltransferase from Erwinia sp. using two different techniques
title Immobilization of glucosyltransferase from Erwinia sp. using two different techniques
spellingShingle Immobilization of glucosyltransferase from Erwinia sp. using two different techniques
Contesini, Fabiano Jares
Erwinia Sp.
Glucosyltransferase
Immobilization
Isomaltulose
Trehalulose
title_short Immobilization of glucosyltransferase from Erwinia sp. using two different techniques
title_full Immobilization of glucosyltransferase from Erwinia sp. using two different techniques
title_fullStr Immobilization of glucosyltransferase from Erwinia sp. using two different techniques
title_full_unstemmed Immobilization of glucosyltransferase from Erwinia sp. using two different techniques
title_sort Immobilization of glucosyltransferase from Erwinia sp. using two different techniques
dc.creator.none.fl_str_mv Contesini, Fabiano Jares
Ibarguren, Carolina
Grosso, Carlos Raimundo Ferreira
de Oliveira Carvalho, Patrícia
Sato, Hélia Harumi
author Contesini, Fabiano Jares
author_facet Contesini, Fabiano Jares
Ibarguren, Carolina
Grosso, Carlos Raimundo Ferreira
de Oliveira Carvalho, Patrícia
Sato, Hélia Harumi
author_role author
author2 Ibarguren, Carolina
Grosso, Carlos Raimundo Ferreira
de Oliveira Carvalho, Patrícia
Sato, Hélia Harumi
author2_role author
author
author
author
dc.subject.none.fl_str_mv Erwinia Sp.
Glucosyltransferase
Immobilization
Isomaltulose
Trehalulose
topic Erwinia Sp.
Glucosyltransferase
Immobilization
Isomaltulose
Trehalulose
purl_subject.fl_str_mv https://purl.org/becyt/ford/2.9
https://purl.org/becyt/ford/2
dc.description.none.fl_txt_mv Two different techniques of glucosyltransferase immobilization were studied for the conversion of sucrose into isomaltulose. The optimum conditions for immobilization of Erwinia sp. glucosyltransferase onto Celite 545, determined using response surface methodology, was pH 4.0 and 170. U. of. glucosyltransferase/g of Celite 545. Using this conditions more than 60% conversion of sucrose into isomaltulose can be obtained. The immobilization of glucosyltransferase was also studied by its entrapment in microcapsules of low-methoxyl pectin and fat (butter and oleic acid). The non-lyophilized microcapsules of pectin, containing the enzyme and fat, showed higher glucosyltransferase activity, compared with lyophilized microcapsules containing enzyme plus fat, and also lyophilized microcapsules containing enzyme without fat addition. The non-lyophilized microcapsules of pectin containing the glucosyltransferase and fat, converted 30% of sucrose into isomaltulose in the first batch. However the conversion decreased to 5% at the 10th batch, indicating inactivation of the enzyme. © 2012 Elsevier B.V.
Fil: Contesini, Fabiano Jares. Universidade Estadual de Campinas; Brasil
Fil: Ibarguren, Carolina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Salta. Instituto de Investigaciones para la Industria Química. Universidad Nacional de Salta. Facultad de Ingeniería. Instituto de Investigaciones para la Industria Química; Argentina
Fil: Grosso, Carlos Raimundo Ferreira. Universidade Estadual de Campinas; Brasil
Fil: de Oliveira Carvalho, Patrícia. University São Francisco; Brasil
Fil: Sato, Hélia Harumi. Universidade Estadual de Campinas; Brasil
description Two different techniques of glucosyltransferase immobilization were studied for the conversion of sucrose into isomaltulose. The optimum conditions for immobilization of Erwinia sp. glucosyltransferase onto Celite 545, determined using response surface methodology, was pH 4.0 and 170. U. of. glucosyltransferase/g of Celite 545. Using this conditions more than 60% conversion of sucrose into isomaltulose can be obtained. The immobilization of glucosyltransferase was also studied by its entrapment in microcapsules of low-methoxyl pectin and fat (butter and oleic acid). The non-lyophilized microcapsules of pectin, containing the enzyme and fat, showed higher glucosyltransferase activity, compared with lyophilized microcapsules containing enzyme plus fat, and also lyophilized microcapsules containing enzyme without fat addition. The non-lyophilized microcapsules of pectin containing the glucosyltransferase and fat, converted 30% of sucrose into isomaltulose in the first batch. However the conversion decreased to 5% at the 10th batch, indicating inactivation of the enzyme. © 2012 Elsevier B.V.
publishDate 2012
dc.date.none.fl_str_mv 2012-04
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/60948
Contesini, Fabiano Jares; Ibarguren, Carolina; Grosso, Carlos Raimundo Ferreira; de Oliveira Carvalho, Patrícia; Sato, Hélia Harumi; Immobilization of glucosyltransferase from Erwinia sp. using two different techniques; Elsevier Science; Journal of Biotechnology; 158; 3; 4-2012; 137-143
0168-1656
CONICET Digital
CONICET
url http://hdl.handle.net/11336/60948
identifier_str_mv Contesini, Fabiano Jares; Ibarguren, Carolina; Grosso, Carlos Raimundo Ferreira; de Oliveira Carvalho, Patrícia; Sato, Hélia Harumi; Immobilization of glucosyltransferase from Erwinia sp. using two different techniques; Elsevier Science; Journal of Biotechnology; 158; 3; 4-2012; 137-143
0168-1656
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1016/j.jbiotec.2012.01.012
info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S016816561200034X
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Elsevier Science
publisher.none.fl_str_mv Elsevier Science
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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score 13.13397

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