New applications of glyoxyl-octyl agarose in lipases co-immobilization: Strategies to reuse the most stable lipase

Lipase B from Candida antarctica (CALB), lipase from Rhizomucor miehei (RML) and phospholipase Lecitase Ultra (LEU) were immobilized via interfacial activation and their stabilities were compared. Immobilized CALB was much more stable than immobilized RML or LEU. That meant that, if they were coimmo...

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Autores: Arana-Peña, Sara, Mendez-Sanchez, Carmen, Rios, Nathalia S., Ortiz, Claudia, Gonçalves, Luciana R. B., Fernández-Lafuente, Roberto
Tipo de recurso: artículo
Estado:Versión aceptada para publicación
Fecha de publicación:2019
País:España
Institución:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/373219
Acceso en línea:http://hdl.handle.net/10261/373219
https://www.scopus.com/inward/record.uri?eid=2-s2.0-85063479579&doi=10.1016%2fj.ijbiomac.2019.03.163&partnerID=40&md5=d3f0ecf520a125de9e26bd233a46301b
Access Level:acceso abierto
Palabra clave:Combilipase
Lipase interfacial activation
Step-by-step immobilization
Glyoxyl-octyl agarose
Lipase desorption
Enzyme reuse
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spelling New applications of glyoxyl-octyl agarose in lipases co-immobilization: Strategies to reuse the most stable lipaseArana-Peña, SaraMendez-Sanchez, CarmenRios, Nathalia S.Ortiz, ClaudiaGonçalves, Luciana R. B.Fernández-Lafuente, RobertoCombilipaseLipase interfacial activationStep-by-step immobilizationGlyoxyl-octyl agaroseLipase desorptionEnzyme reuseLipase B from Candida antarctica (CALB), lipase from Rhizomucor miehei (RML) and phospholipase Lecitase Ultra (LEU) were immobilized via interfacial activation and their stabilities were compared. Immobilized CALB was much more stable than immobilized RML or LEU. That meant that, if they were coimmobilized, after the inactivation of the least stable lipases, CALB should be discarded even though it may maintain full activity. This could be solved by sequential coimmobilization on octyl-glyoxyl (OCGLX). First, CALB was immobilized on OCGLX getting some covalent bonds between most of the CALB molecules and the support. Then, after reduction of CALB immobilized on OCGLX, RML or LEU can be immobilized on the support via interfacial activation. These enzymes could be released from the support just by using detergents, without affecting CALB activity. After optimization of the lipase desorption conditions, the bi-combilipases CALB/RML and CALB/LEU or the triple-combilipase CALB/RML/LEU could be submitted to several cycles of immobilized biocatalyst inactivation, desorption and enzyme reloading keeping the activity of the immobilized CALB almost intact. This way, by using OCGLX and a stepwise immobilization protocol, discarding all coimmobilized lipases when one becomes inactivated is no longer required. Thus, the most stable ones can be reused in several cycles. © 2019 Elsevier B.V.We gratefully recognize the support from the MINECO from Spanish Government, (project number CTQ2017-86170-R) and Colciencias (Colombia) (project number FP 44842-076-2016). Nathalia S. Rios thanks to CNPq for a predoctoral fellowship (CNPq scholarship – Brazil). Mr. Martinez (Novozymes Spain) is gratefully recognized by the donation of the enzymes. The help and suggestions from Dr. Ángel Berenguer (Departamento de Química Inorgánica, Universidad de Alicante) are gratefully recognized.Peer reviewedElsevier BVAgencia Estatal de Investigación (España)Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (Brasil)Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]202420242019info:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_6501Postprintinfo:eu-repo/semantics/acceptedVersionhttp://hdl.handle.net/10261/373219https://www.scopus.com/inward/record.uri?eid=2-s2.0-85063479579&doi=10.1016%2fj.ijbiomac.2019.03.163&partnerID=40&md5=d3f0ecf520a125de9e26bd233a46301breponame:DIGITAL.CSIC. Repositorio Institucional del CSICinstname:Consejo Superior de Investigaciones Científicas (CSIC)Inglés#PLACEHOLDER_PARENT_METADATA_VALUE##PLACEHOLDER_PARENT_METADATA_VALUE#info:eu-repo/grantAgreement/AEI/Plan Estatal de Investigación Científica y Técnica y de Innovación 2013-2016/CTQ2017-86170-Rinfo:eu-repo/grantAgreement/AEI/Plan Estatal de Investigación Científica y Técnica y de Innovación 2013-2016/FP44842-076-2016https://doi.org/10.1016/j.ijbiomac.2019.03.163Síinfo:eu-repo/semantics/openAccessoai:digital.csic.es:10261/3732192026-05-22T06:33:51Z
dc.title.none.fl_str_mv New applications of glyoxyl-octyl agarose in lipases co-immobilization: Strategies to reuse the most stable lipase
title New applications of glyoxyl-octyl agarose in lipases co-immobilization: Strategies to reuse the most stable lipase
spellingShingle New applications of glyoxyl-octyl agarose in lipases co-immobilization: Strategies to reuse the most stable lipase
Arana-Peña, Sara
Combilipase
Lipase interfacial activation
Step-by-step immobilization
Glyoxyl-octyl agarose
Lipase desorption
Enzyme reuse
title_short New applications of glyoxyl-octyl agarose in lipases co-immobilization: Strategies to reuse the most stable lipase
title_full New applications of glyoxyl-octyl agarose in lipases co-immobilization: Strategies to reuse the most stable lipase
title_fullStr New applications of glyoxyl-octyl agarose in lipases co-immobilization: Strategies to reuse the most stable lipase
title_full_unstemmed New applications of glyoxyl-octyl agarose in lipases co-immobilization: Strategies to reuse the most stable lipase
title_sort New applications of glyoxyl-octyl agarose in lipases co-immobilization: Strategies to reuse the most stable lipase
dc.creator.none.fl_str_mv Arana-Peña, Sara
Mendez-Sanchez, Carmen
Rios, Nathalia S.
Ortiz, Claudia
Gonçalves, Luciana R. B.
Fernández-Lafuente, Roberto
author Arana-Peña, Sara
author_facet Arana-Peña, Sara
Mendez-Sanchez, Carmen
Rios, Nathalia S.
Ortiz, Claudia
Gonçalves, Luciana R. B.
Fernández-Lafuente, Roberto
author_role author
author2 Mendez-Sanchez, Carmen
Rios, Nathalia S.
Ortiz, Claudia
Gonçalves, Luciana R. B.
Fernández-Lafuente, Roberto
author2_role author
author
author
author
author
dc.contributor.none.fl_str_mv Agencia Estatal de Investigación (España)
Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (Brasil)
Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]
dc.subject.none.fl_str_mv Combilipase
Lipase interfacial activation
Step-by-step immobilization
Glyoxyl-octyl agarose
Lipase desorption
Enzyme reuse
topic Combilipase
Lipase interfacial activation
Step-by-step immobilization
Glyoxyl-octyl agarose
Lipase desorption
Enzyme reuse
description Lipase B from Candida antarctica (CALB), lipase from Rhizomucor miehei (RML) and phospholipase Lecitase Ultra (LEU) were immobilized via interfacial activation and their stabilities were compared. Immobilized CALB was much more stable than immobilized RML or LEU. That meant that, if they were coimmobilized, after the inactivation of the least stable lipases, CALB should be discarded even though it may maintain full activity. This could be solved by sequential coimmobilization on octyl-glyoxyl (OCGLX). First, CALB was immobilized on OCGLX getting some covalent bonds between most of the CALB molecules and the support. Then, after reduction of CALB immobilized on OCGLX, RML or LEU can be immobilized on the support via interfacial activation. These enzymes could be released from the support just by using detergents, without affecting CALB activity. After optimization of the lipase desorption conditions, the bi-combilipases CALB/RML and CALB/LEU or the triple-combilipase CALB/RML/LEU could be submitted to several cycles of immobilized biocatalyst inactivation, desorption and enzyme reloading keeping the activity of the immobilized CALB almost intact. This way, by using OCGLX and a stepwise immobilization protocol, discarding all coimmobilized lipases when one becomes inactivated is no longer required. Thus, the most stable ones can be reused in several cycles. © 2019 Elsevier B.V.
publishDate 2019
dc.date.none.fl_str_mv 2019
2024
2024
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/10261/373219
https://www.scopus.com/inward/record.uri?eid=2-s2.0-85063479579&doi=10.1016%2fj.ijbiomac.2019.03.163&partnerID=40&md5=d3f0ecf520a125de9e26bd233a46301b
url http://hdl.handle.net/10261/373219
https://www.scopus.com/inward/record.uri?eid=2-s2.0-85063479579&doi=10.1016%2fj.ijbiomac.2019.03.163&partnerID=40&md5=d3f0ecf520a125de9e26bd233a46301b
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv #PLACEHOLDER_PARENT_METADATA_VALUE#
#PLACEHOLDER_PARENT_METADATA_VALUE#
info:eu-repo/grantAgreement/AEI/Plan Estatal de Investigación Científica y Técnica y de Innovación 2013-2016/CTQ2017-86170-R
info:eu-repo/grantAgreement/AEI/Plan Estatal de Investigación Científica y Técnica y de Innovación 2013-2016/FP44842-076-2016
https://doi.org/10.1016/j.ijbiomac.2019.03.163
Sí
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.publisher.none.fl_str_mv Elsevier BV
publisher.none.fl_str_mv Elsevier BV
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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