Cyclodextrin glycosyltransferase from Bacillus circulans DF 9R: Activity and kinetic studies

Autores
Szerman, Natalia; Rodríguez Gastón, Jorgelina Andrea; Costa, Hernán; Krymkiewicz, Norberto; Ferrarotti, Susana Alicia
Año de publicación
2009
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Activity characteristics and kinetic aspects of a cyclodextrin glycosyltransferase (CGTase) from Bacillus circulans DF 9R were studied. A mixture of α-, β- and γ-cyclodextrins (CDs), glucose, maltose and negligible amounts of longer linear dextrins were produced from gelatinized amylose, amylopectin and starch from different sources. In the coupling reaction, CDs were the substrates in the presence of acceptors such as maltose and/or longer oligosaccharides. From oligosaccharides formed by three or more glucose units, this enzyme produced linear chains of several lengths which were then cyclized. CGTase catalytic efficiency was compared employing an analytical grade starch and cassava starch for food use. Since the results obtained were similar for both starches, the use of an economic starch is an advantage. CGTase was inhibited by the substrate and its own products. Starch concentrations over 20 mg/mL inhibited the cyclizing activity. CDs behaved as competitive inhibitors and maltose as an uncompetitive inhibitor while maltotriose showed a mixed inhibition pattern. Limit dextrins showed a scarce inhibitory effect on enzyme activity. CD production could be improved with an ultrafiltration membrane reactor for continuous removal of the products; the starch concentration should be maintained below an inhibitory concentration and limit dextrins would remain in the reactor without affecting enzyme activity.
Fil: Szerman, Natalia. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Tecnología de Alimentos; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Luján. Departamento de Ciencias Básicas; Argentina.
Fil: Rodríguez Gastón, Jorgelina Andrea. Universidad Nacional de Luján. Departamento de Ciencias Básicas; Argentina.
Fil: Costa, Hernán. Universidad Nacional de Luján. Departamento de Ciencias Básicas; Argentina.
Fil: Krymkiewicz, Norberto. Universidad Nacional de Luján. Departamento de Ciencias Básicas; Argentina.
Fil: Ferrarotti, Susana Alicia. Universidad Nacional de Luján. Departamento de Ciencias Básicas; Argentina.
Fuente
Enzyme and Microbial Technology 45 (1) : 36-41 (July 2009)
Materia
Cyclodextrins
Glycosyltransferases
Ciclodextrinas
Glicosiltransferasas
Bacillus circulans
Cyclodextrin glycosyltransferase
Kinetic parameters
Ciclodextrina glicosiltransferasa
Parámetros cinéticos
Bacillus circulans DF 9R
Nivel de accesibilidad
acceso restringido
Condiciones de uso
Repositorio
INTA Digital (INTA)
Institución
Instituto Nacional de Tecnología Agropecuaria
OAI Identificador
oai:localhost:20.500.12123/5950
Acceder
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oai_identifier_str oai:localhost:20.500.12123/5950
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network_name_str INTA Digital (INTA)
spelling Cyclodextrin glycosyltransferase from Bacillus circulans DF 9R: Activity and kinetic studiesSzerman, NataliaRodríguez Gastón, Jorgelina AndreaCosta, HernánKrymkiewicz, NorbertoFerrarotti, Susana AliciaCyclodextrinsGlycosyltransferasesCiclodextrinasGlicosiltransferasasBacillus circulansCyclodextrin glycosyltransferaseKinetic parametersCiclodextrina glicosiltransferasaParámetros cinéticosBacillus circulans DF 9RActivity characteristics and kinetic aspects of a cyclodextrin glycosyltransferase (CGTase) from Bacillus circulans DF 9R were studied. A mixture of α-, β- and γ-cyclodextrins (CDs), glucose, maltose and negligible amounts of longer linear dextrins were produced from gelatinized amylose, amylopectin and starch from different sources. In the coupling reaction, CDs were the substrates in the presence of acceptors such as maltose and/or longer oligosaccharides. From oligosaccharides formed by three or more glucose units, this enzyme produced linear chains of several lengths which were then cyclized. CGTase catalytic efficiency was compared employing an analytical grade starch and cassava starch for food use. Since the results obtained were similar for both starches, the use of an economic starch is an advantage. CGTase was inhibited by the substrate and its own products. Starch concentrations over 20 mg/mL inhibited the cyclizing activity. CDs behaved as competitive inhibitors and maltose as an uncompetitive inhibitor while maltotriose showed a mixed inhibition pattern. Limit dextrins showed a scarce inhibitory effect on enzyme activity. CD production could be improved with an ultrafiltration membrane reactor for continuous removal of the products; the starch concentration should be maintained below an inhibitory concentration and limit dextrins would remain in the reactor without affecting enzyme activity.Fil: Szerman, Natalia. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Tecnología de Alimentos; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Luján. Departamento de Ciencias Básicas; Argentina.Fil: Rodríguez Gastón, Jorgelina Andrea. Universidad Nacional de Luján. Departamento de Ciencias Básicas; Argentina.Fil: Costa, Hernán. Universidad Nacional de Luján. Departamento de Ciencias Básicas; Argentina.Fil: Krymkiewicz, Norberto. Universidad Nacional de Luján. Departamento de Ciencias Básicas; Argentina.Fil: Ferrarotti, Susana Alicia. Universidad Nacional de Luján. Departamento de Ciencias Básicas; Argentina.Elsevier2019-09-24T11:05:29Z2019-09-24T11:05:29Z2009-07info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfhttps://www.sciencedirect.com/science/article/pii/S0141022909000854http://hdl.handle.net/20.500.12123/59500141-0229https://doi.org/10.1016/j.enzmictec.2009.04.002Enzyme and Microbial Technology 45 (1) : 36-41 (July 2009)reponame:INTA Digital (INTA)instname:Instituto Nacional de Tecnología Agropecuariaenginfo:eu-repo/semantics/restrictedAccess2025-09-11T10:23:11Zoai:localhost:20.500.12123/5950instacron:INTAInstitucionalhttp://repositorio.inta.gob.ar/Organismo científico-tecnológicoNo correspondehttp://repositorio.inta.gob.ar/oai/requesttripaldi.nicolas@inta.gob.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:l2025-09-11 10:23:11.424INTA Digital (INTA) - Instituto Nacional de Tecnología Agropecuariafalse
dc.title.none.fl_str_mv Cyclodextrin glycosyltransferase from Bacillus circulans DF 9R: Activity and kinetic studies
title Cyclodextrin glycosyltransferase from Bacillus circulans DF 9R: Activity and kinetic studies
spellingShingle Cyclodextrin glycosyltransferase from Bacillus circulans DF 9R: Activity and kinetic studies
Szerman, Natalia
Cyclodextrins
Glycosyltransferases
Ciclodextrinas
Glicosiltransferasas
Bacillus circulans
Cyclodextrin glycosyltransferase
Kinetic parameters
Ciclodextrina glicosiltransferasa
Parámetros cinéticos
Bacillus circulans DF 9R
title_short Cyclodextrin glycosyltransferase from Bacillus circulans DF 9R: Activity and kinetic studies
title_full Cyclodextrin glycosyltransferase from Bacillus circulans DF 9R: Activity and kinetic studies
title_fullStr Cyclodextrin glycosyltransferase from Bacillus circulans DF 9R: Activity and kinetic studies
title_full_unstemmed Cyclodextrin glycosyltransferase from Bacillus circulans DF 9R: Activity and kinetic studies
title_sort Cyclodextrin glycosyltransferase from Bacillus circulans DF 9R: Activity and kinetic studies
dc.creator.none.fl_str_mv Szerman, Natalia
Rodríguez Gastón, Jorgelina Andrea
Costa, Hernán
Krymkiewicz, Norberto
Ferrarotti, Susana Alicia
author Szerman, Natalia
author_facet Szerman, Natalia
Rodríguez Gastón, Jorgelina Andrea
Costa, Hernán
Krymkiewicz, Norberto
Ferrarotti, Susana Alicia
author_role author
author2 Rodríguez Gastón, Jorgelina Andrea
Costa, Hernán
Krymkiewicz, Norberto
Ferrarotti, Susana Alicia
author2_role author
author
author
author
dc.subject.none.fl_str_mv Cyclodextrins
Glycosyltransferases
Ciclodextrinas
Glicosiltransferasas
Bacillus circulans
Cyclodextrin glycosyltransferase
Kinetic parameters
Ciclodextrina glicosiltransferasa
Parámetros cinéticos
Bacillus circulans DF 9R
topic Cyclodextrins
Glycosyltransferases
Ciclodextrinas
Glicosiltransferasas
Bacillus circulans
Cyclodextrin glycosyltransferase
Kinetic parameters
Ciclodextrina glicosiltransferasa
Parámetros cinéticos
Bacillus circulans DF 9R
dc.description.none.fl_txt_mv Activity characteristics and kinetic aspects of a cyclodextrin glycosyltransferase (CGTase) from Bacillus circulans DF 9R were studied. A mixture of α-, β- and γ-cyclodextrins (CDs), glucose, maltose and negligible amounts of longer linear dextrins were produced from gelatinized amylose, amylopectin and starch from different sources. In the coupling reaction, CDs were the substrates in the presence of acceptors such as maltose and/or longer oligosaccharides. From oligosaccharides formed by three or more glucose units, this enzyme produced linear chains of several lengths which were then cyclized. CGTase catalytic efficiency was compared employing an analytical grade starch and cassava starch for food use. Since the results obtained were similar for both starches, the use of an economic starch is an advantage. CGTase was inhibited by the substrate and its own products. Starch concentrations over 20 mg/mL inhibited the cyclizing activity. CDs behaved as competitive inhibitors and maltose as an uncompetitive inhibitor while maltotriose showed a mixed inhibition pattern. Limit dextrins showed a scarce inhibitory effect on enzyme activity. CD production could be improved with an ultrafiltration membrane reactor for continuous removal of the products; the starch concentration should be maintained below an inhibitory concentration and limit dextrins would remain in the reactor without affecting enzyme activity.
Fil: Szerman, Natalia. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Tecnología de Alimentos; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Luján. Departamento de Ciencias Básicas; Argentina.
Fil: Rodríguez Gastón, Jorgelina Andrea. Universidad Nacional de Luján. Departamento de Ciencias Básicas; Argentina.
Fil: Costa, Hernán. Universidad Nacional de Luján. Departamento de Ciencias Básicas; Argentina.
Fil: Krymkiewicz, Norberto. Universidad Nacional de Luján. Departamento de Ciencias Básicas; Argentina.
Fil: Ferrarotti, Susana Alicia. Universidad Nacional de Luján. Departamento de Ciencias Básicas; Argentina.
description Activity characteristics and kinetic aspects of a cyclodextrin glycosyltransferase (CGTase) from Bacillus circulans DF 9R were studied. A mixture of α-, β- and γ-cyclodextrins (CDs), glucose, maltose and negligible amounts of longer linear dextrins were produced from gelatinized amylose, amylopectin and starch from different sources. In the coupling reaction, CDs were the substrates in the presence of acceptors such as maltose and/or longer oligosaccharides. From oligosaccharides formed by three or more glucose units, this enzyme produced linear chains of several lengths which were then cyclized. CGTase catalytic efficiency was compared employing an analytical grade starch and cassava starch for food use. Since the results obtained were similar for both starches, the use of an economic starch is an advantage. CGTase was inhibited by the substrate and its own products. Starch concentrations over 20 mg/mL inhibited the cyclizing activity. CDs behaved as competitive inhibitors and maltose as an uncompetitive inhibitor while maltotriose showed a mixed inhibition pattern. Limit dextrins showed a scarce inhibitory effect on enzyme activity. CD production could be improved with an ultrafiltration membrane reactor for continuous removal of the products; the starch concentration should be maintained below an inhibitory concentration and limit dextrins would remain in the reactor without affecting enzyme activity.
publishDate 2009
dc.date.none.fl_str_mv 2009-07
2019-09-24T11:05:29Z
2019-09-24T11:05:29Z
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 https://www.sciencedirect.com/science/article/pii/S0141022909000854
http://hdl.handle.net/20.500.12123/5950
0141-0229
https://doi.org/10.1016/j.enzmictec.2009.04.002
url https://www.sciencedirect.com/science/article/pii/S0141022909000854
http://hdl.handle.net/20.500.12123/5950
https://doi.org/10.1016/j.enzmictec.2009.04.002
identifier_str_mv 0141-0229
dc.language.none.fl_str_mv eng
language eng
dc.rights.none.fl_str_mv info:eu-repo/semantics/restrictedAccess
eu_rights_str_mv restrictedAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv Elsevier
publisher.none.fl_str_mv Elsevier
dc.source.none.fl_str_mv Enzyme and Microbial Technology 45 (1) : 36-41 (July 2009)
reponame:INTA Digital (INTA)
instname:Instituto Nacional de Tecnología Agropecuaria
reponame_str INTA Digital (INTA)
collection INTA Digital (INTA)
instname_str Instituto Nacional de Tecnología Agropecuaria
repository.name.fl_str_mv INTA Digital (INTA) - Instituto Nacional de Tecnología Agropecuaria
repository.mail.fl_str_mv tripaldi.nicolas@inta.gob.ar
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score 12.993085

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