Immobilization of the glucose isomerase from Caldicoprobacter algeriensis on Sepabeads EC-HA and its efficient application in continuous High Fructose Syrup production using packed bed reactor

[EN] The glucose isomerase GICA from Caldicoprobacter algeriensis was immobilized by ionic adsorption on polymethacrylate carriers (Sepabeads EC-EA and EC-HA) or covalent attachment to glyoxal agarose. The Sepabeads EC-HA yielded the highest recovery of activity (89%). The optimum temperature and pH...

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Autores: Neifar, Sawssan, Cervantes, Fadia V., BenHlima, Hajer, Bouanane-Darenfed, Amel, Ballesteros Olmo, Antonio, Plou Gasca, Francisco José, Bejar, Samir
Tipo de recurso: artículo
Estado:Versión aceptada para publicación
Fecha de publicación:2020
País:España
Institución:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/216977
Acceso en línea:http://hdl.handle.net/10261/216977
Access Level:acceso abierto
Palabra clave:Glucose isomerase
Enzyme immobilization
Sepabeads
Batch reactor
Packed Bed Reactor
HFS
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spelling Immobilization of the glucose isomerase from Caldicoprobacter algeriensis on Sepabeads EC-HA and its efficient application in continuous High Fructose Syrup production using packed bed reactorNeifar, SawssanCervantes, Fadia V.BenHlima, HajerBouanane-Darenfed, AmelBallesteros Olmo, AntonioPlou Gasca, Francisco JoséBejar, SamirGlucose isomeraseEnzyme immobilizationSepabeadsBatch reactorPacked Bed ReactorHFS[EN] The glucose isomerase GICA from Caldicoprobacter algeriensis was immobilized by ionic adsorption on polymethacrylate carriers (Sepabeads EC-EA and EC-HA) or covalent attachment to glyoxal agarose. The Sepabeads EC-HA yielded the highest recovery of activity (89%). The optimum temperature and pH of immobilized GICA were 90 °C and 7.0, respectively, similar to the corresponding values of free enzyme. Nevertheless, the adsorbed enzyme displayed higher relative activity at acidic pH, greater thermostability, and better storage stability, compared to the free form. Moreover, the immobilized enzyme showed an excellent operational stability, in 15 successive 3 h reaction cycles at 85 °C under a batch reactor, preserving 83% of its initial activity. Interestingly, a continuous process for High Fructose Syrup (HFS) production was established with the adsorbed GICA using a packed bed reactor during eleven days at 70 °C. HPAEC-PAD analysis showed a maximum bioconversion rate of 49% after 48 h of operation.This work was supported by the Tunisian Ministry of Higher Education and Scientific Research and Technology (contract program LBMIE-CBS, code: LR15CBS06), University of Sfax (doctoral school of FSS) and the Spanish Ministry of Economy and Competitiveness (Grant BIO2016-76601-C3-1-R).ElsevierMinistère de l’Enseignement Supérieur et de la Recherche Scientifique (Tunisie)Université de SfaxMinisterio de Economía y Competitividad (España)Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]2020202020202020info:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_6501Postprintinfo:eu-repo/semantics/acceptedVersionhttp://hdl.handle.net/10261/216977reponame:DIGITAL.CSIC. Repositorio Institucional del CSICinstname:Consejo Superior de Investigaciones Científicas (CSIC)Inglés#PLACEHOLDER_PARENT_METADATA_VALUE#info:eu-repo/grantAgreement/MINECO/Plan Estatal de Investigación Científica y Técnica y de Innovación 2013-2016/BIO2016-76601-C3-1-Rhttp://dx.doi.org/10.1016/j.foodchem.2019.125710Síinfo:eu-repo/semantics/openAccessoai:digital.csic.es:10261/2169772026-05-22T06:33:51Z
dc.title.none.fl_str_mv Immobilization of the glucose isomerase from Caldicoprobacter algeriensis on Sepabeads EC-HA and its efficient application in continuous High Fructose Syrup production using packed bed reactor
title Immobilization of the glucose isomerase from Caldicoprobacter algeriensis on Sepabeads EC-HA and its efficient application in continuous High Fructose Syrup production using packed bed reactor
spellingShingle Immobilization of the glucose isomerase from Caldicoprobacter algeriensis on Sepabeads EC-HA and its efficient application in continuous High Fructose Syrup production using packed bed reactor
Neifar, Sawssan
Glucose isomerase
Enzyme immobilization
Sepabeads
Batch reactor
Packed Bed Reactor
HFS
title_short Immobilization of the glucose isomerase from Caldicoprobacter algeriensis on Sepabeads EC-HA and its efficient application in continuous High Fructose Syrup production using packed bed reactor
title_full Immobilization of the glucose isomerase from Caldicoprobacter algeriensis on Sepabeads EC-HA and its efficient application in continuous High Fructose Syrup production using packed bed reactor
title_fullStr Immobilization of the glucose isomerase from Caldicoprobacter algeriensis on Sepabeads EC-HA and its efficient application in continuous High Fructose Syrup production using packed bed reactor
title_full_unstemmed Immobilization of the glucose isomerase from Caldicoprobacter algeriensis on Sepabeads EC-HA and its efficient application in continuous High Fructose Syrup production using packed bed reactor
title_sort Immobilization of the glucose isomerase from Caldicoprobacter algeriensis on Sepabeads EC-HA and its efficient application in continuous High Fructose Syrup production using packed bed reactor
dc.creator.none.fl_str_mv Neifar, Sawssan
Cervantes, Fadia V.
BenHlima, Hajer
Bouanane-Darenfed, Amel
Ballesteros Olmo, Antonio
Plou Gasca, Francisco José
Bejar, Samir
author Neifar, Sawssan
author_facet Neifar, Sawssan
Cervantes, Fadia V.
BenHlima, Hajer
Bouanane-Darenfed, Amel
Ballesteros Olmo, Antonio
Plou Gasca, Francisco José
Bejar, Samir
author_role author
author2 Cervantes, Fadia V.
BenHlima, Hajer
Bouanane-Darenfed, Amel
Ballesteros Olmo, Antonio
Plou Gasca, Francisco José
Bejar, Samir
author2_role author
author
author
author
author
author
dc.contributor.none.fl_str_mv Ministère de l’Enseignement Supérieur et de la Recherche Scientifique (Tunisie)
Université de Sfax
Ministerio de Economía y Competitividad (España)
Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]
dc.subject.none.fl_str_mv Glucose isomerase
Enzyme immobilization
Sepabeads
Batch reactor
Packed Bed Reactor
HFS
topic Glucose isomerase
Enzyme immobilization
Sepabeads
Batch reactor
Packed Bed Reactor
HFS
description [EN] The glucose isomerase GICA from Caldicoprobacter algeriensis was immobilized by ionic adsorption on polymethacrylate carriers (Sepabeads EC-EA and EC-HA) or covalent attachment to glyoxal agarose. The Sepabeads EC-HA yielded the highest recovery of activity (89%). The optimum temperature and pH of immobilized GICA were 90 °C and 7.0, respectively, similar to the corresponding values of free enzyme. Nevertheless, the adsorbed enzyme displayed higher relative activity at acidic pH, greater thermostability, and better storage stability, compared to the free form. Moreover, the immobilized enzyme showed an excellent operational stability, in 15 successive 3 h reaction cycles at 85 °C under a batch reactor, preserving 83% of its initial activity. Interestingly, a continuous process for High Fructose Syrup (HFS) production was established with the adsorbed GICA using a packed bed reactor during eleven days at 70 °C. HPAEC-PAD analysis showed a maximum bioconversion rate of 49% after 48 h of operation.
publishDate 2020
dc.date.none.fl_str_mv 2020
2020
2020
2020
dc.type.none.fl_str_mv info:eu-repo/semantics/article
http://purl.org/coar/resource_type/c_6501
Postprint
info:eu-repo/semantics/acceptedVersion
format article
status_str acceptedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/10261/216977
url http://hdl.handle.net/10261/216977
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv #PLACEHOLDER_PARENT_METADATA_VALUE#
info:eu-repo/grantAgreement/MINECO/Plan Estatal de Investigación Científica y Técnica y de Innovación 2013-2016/BIO2016-76601-C3-1-R
http://dx.doi.org/10.1016/j.foodchem.2019.125710
Sí
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.publisher.none.fl_str_mv Elsevier
publisher.none.fl_str_mv Elsevier
dc.source.none.fl_str_mv reponame:DIGITAL.CSIC. Repositorio Institucional del CSIC
instname:Consejo Superior de Investigaciones Científicas (CSIC)
instname_str Consejo Superior de Investigaciones Científicas (CSIC)
reponame_str DIGITAL.CSIC. Repositorio Institucional del CSIC
collection DIGITAL.CSIC. Repositorio Institucional del CSIC
repository.name.fl_str_mv
repository.mail.fl_str_mv
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score 15,811543

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