Invertase from a strain of Rhodotorula glutinis

Autores
Rubio, María Cristina; Runco, Rosa; Navarro, Antonio Roberto
Año de publicación
2002
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
An invertase (β-D-fructofuranoside fructohydrolase, EC 3.2.1.26) from Rhodotorula glutinis was purified by ammonium sulfate fractionation, gel filtration and anion exchange chromatography. Invertase molecular weight was estimated to be 100 kDa by analytical gel filtration and 47 kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). Molecular mass determinations indicated that the native enzyme exists as a homodimer. It is a glycoprotein that contains 19% carbohydrate. The enzyme attacks β-D-fructofuranoside (raffinose, stachyose and sucrose) from the fructose end. It has a Km of 0.227 M and a Vmax of 0.096 μmol/min with sucrose as a substrate. Invertase activity is stable between pH 2.6 and 5.5 for 30 min, maximum activity being observed at pH 4.5. The activation energy was 6520 cal/mol. The enzyme is stable between 20 and 60°C. Mg2+ and Ca2+ ions stimulated invertase activity 3-fold, while Fe2+, K+, Co2+, Na+ and Cu2+ increased activity about 2-fold. The transfructosylation reaction could not be observed. This enzyme is of particular interest since it appears to have a high hydrolytic activity in 1 M sucrose solution. This fact would make the enzymatic hydrolysis process economically efficient for syrup production using by-products with high salt and sugar contents such as sugar cane molasses. © 2002 Elsevier Science Ltd. All rights reserved.
Fil: Rubio, María Cristina. Universidad Nacional de Tucumán. Facultad de Bioquímica, Química y Farmacia; Argentina
Fil: Runco, Rosa. Universidad Nacional de Tucumán. Facultad de Bioquímica, Química y Farmacia; Argentina
Fil: Navarro, Antonio Roberto. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Tucumán. Facultad de Bioquímica, Química y Farmacia; Argentina
Materia
Β-Fructofuranoside Fructohydrolase
Enzymatic Characterization
Food Industry
Hemiascomycetidae
Invert Sugars
Invertase
Rhodotorula Glutinis
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:11336/79116
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/79116
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Invertase from a strain of Rhodotorula glutinisRubio, María CristinaRunco, RosaNavarro, Antonio RobertoΒ-Fructofuranoside FructohydrolaseEnzymatic CharacterizationFood IndustryHemiascomycetidaeInvert SugarsInvertaseRhodotorula Glutinishttps://purl.org/becyt/ford/2.9https://purl.org/becyt/ford/2An invertase (β-D-fructofuranoside fructohydrolase, EC 3.2.1.26) from Rhodotorula glutinis was purified by ammonium sulfate fractionation, gel filtration and anion exchange chromatography. Invertase molecular weight was estimated to be 100 kDa by analytical gel filtration and 47 kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). Molecular mass determinations indicated that the native enzyme exists as a homodimer. It is a glycoprotein that contains 19% carbohydrate. The enzyme attacks β-D-fructofuranoside (raffinose, stachyose and sucrose) from the fructose end. It has a Km of 0.227 M and a Vmax of 0.096 μmol/min with sucrose as a substrate. Invertase activity is stable between pH 2.6 and 5.5 for 30 min, maximum activity being observed at pH 4.5. The activation energy was 6520 cal/mol. The enzyme is stable between 20 and 60°C. Mg2+ and Ca2+ ions stimulated invertase activity 3-fold, while Fe2+, K+, Co2+, Na+ and Cu2+ increased activity about 2-fold. The transfructosylation reaction could not be observed. This enzyme is of particular interest since it appears to have a high hydrolytic activity in 1 M sucrose solution. This fact would make the enzymatic hydrolysis process economically efficient for syrup production using by-products with high salt and sugar contents such as sugar cane molasses. © 2002 Elsevier Science Ltd. All rights reserved.Fil: Rubio, María Cristina. Universidad Nacional de Tucumán. Facultad de Bioquímica, Química y Farmacia; ArgentinaFil: Runco, Rosa. Universidad Nacional de Tucumán. Facultad de Bioquímica, Química y Farmacia; ArgentinaFil: Navarro, Antonio Roberto. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Tucumán. Facultad de Bioquímica, Química y Farmacia; ArgentinaPergamon-Elsevier Science Ltd2002-11info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdftext/richtextapplication/pdfhttp://hdl.handle.net/11336/79116Rubio, María Cristina; Runco, Rosa; Navarro, Antonio Roberto; Invertase from a strain of Rhodotorula glutinis; Pergamon-Elsevier Science Ltd; Phytochemistry; 61; 6; 11-2002; 605-6090031-9422CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1016/S0031-9422(02)00336-9info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0031942202003369info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:26:56Zoai:ri.conicet.gov.ar:11336/79116instacron: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:34982025-09-29 10:26:56.886CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Invertase from a strain of Rhodotorula glutinis
title Invertase from a strain of Rhodotorula glutinis
spellingShingle Invertase from a strain of Rhodotorula glutinis
Rubio, María Cristina
Β-Fructofuranoside Fructohydrolase
Enzymatic Characterization
Food Industry
Hemiascomycetidae
Invert Sugars
Invertase
Rhodotorula Glutinis
title_short Invertase from a strain of Rhodotorula glutinis
title_full Invertase from a strain of Rhodotorula glutinis
title_fullStr Invertase from a strain of Rhodotorula glutinis
title_full_unstemmed Invertase from a strain of Rhodotorula glutinis
title_sort Invertase from a strain of Rhodotorula glutinis
dc.creator.none.fl_str_mv Rubio, María Cristina
Runco, Rosa
Navarro, Antonio Roberto
author Rubio, María Cristina
author_facet Rubio, María Cristina
Runco, Rosa
Navarro, Antonio Roberto
author_role author
author2 Runco, Rosa
Navarro, Antonio Roberto
author2_role author
author
dc.subject.none.fl_str_mv Β-Fructofuranoside Fructohydrolase
Enzymatic Characterization
Food Industry
Hemiascomycetidae
Invert Sugars
Invertase
Rhodotorula Glutinis
topic Β-Fructofuranoside Fructohydrolase
Enzymatic Characterization
Food Industry
Hemiascomycetidae
Invert Sugars
Invertase
Rhodotorula Glutinis
purl_subject.fl_str_mv https://purl.org/becyt/ford/2.9
https://purl.org/becyt/ford/2
dc.description.none.fl_txt_mv An invertase (β-D-fructofuranoside fructohydrolase, EC 3.2.1.26) from Rhodotorula glutinis was purified by ammonium sulfate fractionation, gel filtration and anion exchange chromatography. Invertase molecular weight was estimated to be 100 kDa by analytical gel filtration and 47 kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). Molecular mass determinations indicated that the native enzyme exists as a homodimer. It is a glycoprotein that contains 19% carbohydrate. The enzyme attacks β-D-fructofuranoside (raffinose, stachyose and sucrose) from the fructose end. It has a Km of 0.227 M and a Vmax of 0.096 μmol/min with sucrose as a substrate. Invertase activity is stable between pH 2.6 and 5.5 for 30 min, maximum activity being observed at pH 4.5. The activation energy was 6520 cal/mol. The enzyme is stable between 20 and 60°C. Mg2+ and Ca2+ ions stimulated invertase activity 3-fold, while Fe2+, K+, Co2+, Na+ and Cu2+ increased activity about 2-fold. The transfructosylation reaction could not be observed. This enzyme is of particular interest since it appears to have a high hydrolytic activity in 1 M sucrose solution. This fact would make the enzymatic hydrolysis process economically efficient for syrup production using by-products with high salt and sugar contents such as sugar cane molasses. © 2002 Elsevier Science Ltd. All rights reserved.
Fil: Rubio, María Cristina. Universidad Nacional de Tucumán. Facultad de Bioquímica, Química y Farmacia; Argentina
Fil: Runco, Rosa. Universidad Nacional de Tucumán. Facultad de Bioquímica, Química y Farmacia; Argentina
Fil: Navarro, Antonio Roberto. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Tucumán. Facultad de Bioquímica, Química y Farmacia; Argentina
description An invertase (β-D-fructofuranoside fructohydrolase, EC 3.2.1.26) from Rhodotorula glutinis was purified by ammonium sulfate fractionation, gel filtration and anion exchange chromatography. Invertase molecular weight was estimated to be 100 kDa by analytical gel filtration and 47 kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). Molecular mass determinations indicated that the native enzyme exists as a homodimer. It is a glycoprotein that contains 19% carbohydrate. The enzyme attacks β-D-fructofuranoside (raffinose, stachyose and sucrose) from the fructose end. It has a Km of 0.227 M and a Vmax of 0.096 μmol/min with sucrose as a substrate. Invertase activity is stable between pH 2.6 and 5.5 for 30 min, maximum activity being observed at pH 4.5. The activation energy was 6520 cal/mol. The enzyme is stable between 20 and 60°C. Mg2+ and Ca2+ ions stimulated invertase activity 3-fold, while Fe2+, K+, Co2+, Na+ and Cu2+ increased activity about 2-fold. The transfructosylation reaction could not be observed. This enzyme is of particular interest since it appears to have a high hydrolytic activity in 1 M sucrose solution. This fact would make the enzymatic hydrolysis process economically efficient for syrup production using by-products with high salt and sugar contents such as sugar cane molasses. © 2002 Elsevier Science Ltd. All rights reserved.
publishDate 2002
dc.date.none.fl_str_mv 2002-11
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/11336/79116
Rubio, María Cristina; Runco, Rosa; Navarro, Antonio Roberto; Invertase from a strain of Rhodotorula glutinis; Pergamon-Elsevier Science Ltd; Phytochemistry; 61; 6; 11-2002; 605-609
0031-9422
CONICET Digital
CONICET
url http://hdl.handle.net/11336/79116
identifier_str_mv Rubio, María Cristina; Runco, Rosa; Navarro, Antonio Roberto; Invertase from a strain of Rhodotorula glutinis; Pergamon-Elsevier Science Ltd; Phytochemistry; 61; 6; 11-2002; 605-609
0031-9422
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/S0031-9422(02)00336-9
info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0031942202003369
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
text/richtext
application/pdf
dc.publisher.none.fl_str_mv Pergamon-Elsevier Science Ltd
publisher.none.fl_str_mv Pergamon-Elsevier Science Ltd
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 13.070432

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