Influence of phosphate anions on the stability of immobilized enzymes. Effect of enzyme nature, immobilization protocol and inactivation conditions

Detalhes bibliográficos
Autor(a) principal: Kornecki, Jakub F.
Data de Publicação: 2020
Outros Autores: Carballares, Diego, Sterlinga, Roberto Morellon, Siar, El Hocine, Kashefi, Saeid, Chafiaa, Mazri, Peña, Sara Arana, Rios, Nathalia Saraiva, Gonçalves, Luciana Rocha Barros, Lafuente, Roberto Fernandez
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Institucional da UFRN
Texto Completo: https://repositorio.ufrn.br/handle/123456789/45070
Resumo: 2030-12
id UFRN_a147538f4153357ee16df19c0e262dbb
oai_identifier_str oai:https://repositorio.ufrn.br:123456789/45070
network_acronym_str UFRN
network_name_str Repositório Institucional da UFRN
repository_id_str
spelling Kornecki, Jakub F.Carballares, DiegoSterlinga, Roberto MorellonSiar, El HocineKashefi, SaeidChafiaa, MazriPeña, Sara AranaRios, Nathalia SaraivaGonçalves, Luciana Rocha BarrosLafuente, Roberto Fernandez2021-11-29T21:30:36Z2020-08KORNECKI, Jakub F.; CARBALLARES, Diego; MORELLON-STERLING, Roberto; SIAR, El Hocine; KASHEFI, Saeid; CHAFIAA, Mazri; ARANA-PEÑA, Sara; RIOS, Nathalia S.; GONÇALVES, Luciana R.B.; FERNANDEZ-LAFUENTE, Roberto. Influence of phosphate anions on the stability of immobilized enzymes. Effect of enzyme nature, immobilization protocol and inactivation conditions. Process Biochemistry, [S.L.], v. 95, p. 288-296, ago. 2020. Disponível em: https://www.sciencedirect.com/science/article/abs/pii/S1359511320301161?via%3Dihub#!. Acesso em: 29 nov. 2021.https://doi.org/10.1016/j.procbio.2020.02.0251359-5113https://repositorio.ufrn.br/handle/123456789/4507010.1016/j.procbio.2020.02.025ElsevierLipase interfacial activationEnzyme destabilizationImmobilized enzyme stabilityBuffers and enzyme stabilityTuning enzyme stability by immobilizationInfluence of phosphate anions on the stability of immobilized enzymes. Effect of enzyme nature, immobilization protocol and inactivation conditionsinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article2030-12A destabilizing effect at pH 7 of sodium phosphate on several lipases immobilized via interfacial activation is shown in this work. This paper investigates if this destabilizing effect is extended to other inactivation conditions, immobilization protocols or even other immobilized enzymes (ficin, trypsin, β-galactosidase, β-glucosidase, laccase, glucose oxidase and catalase). As lipases, those from Candida antarctica (A and B), Candida rugosa and Rhizomucor miehei have been used. Results confirm the very negative effect of 100 mM sodium phosphate at pH 7.0 for the stability of all studied lipases immobilized on octyl agarose, while using glutaraldehyde-support the effect is smaller (still very significant using CALA) and in some cases the effect disappeared (e.g., using CALB). The change of the pH to 5.0 or 9.0, or the addition of 1 M NaCl reduced the negative effect of the phosphate in some instances (e.g., at pH 5.0, this negative effect is only relevant for CALB). Regarding the other enzymes, only the monomeric β-galactosidase from Aspergillus oryzae is strongly destabilized by the phosphate buffer. This way, the immobilization protocol and the inactivation conditions strongly modulate the negative effect of sodium phosphate on the stability of immobilized lipases, and this effect is not extended to other enzymesengreponame:Repositório Institucional da UFRNinstname:Universidade Federal do Rio Grande do Norte (UFRN)instacron:UFRNinfo:eu-repo/semantics/openAccessCC-LICENSElicense_rdflicense_rdfapplication/rdf+xml; charset=utf-8914https://repositorio.ufrn.br/bitstream/123456789/45070/2/license_rdf4d2950bda3d176f570a9f8b328dfbbefMD52LICENSElicense.txtlicense.txttext/plain; charset=utf-81569https://repositorio.ufrn.br/bitstream/123456789/45070/3/license.txt6e6f57145bc87daf99079f06b081ff9fMD53123456789/450702024-03-19 01:05:47.184oai:https://repositorio.ufrn.br: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ório de PublicaçõesPUBhttp://repositorio.ufrn.br/oai/opendoar:2024-03-19T04:05:47Repositório Institucional da UFRN - Universidade Federal do Rio Grande do Norte (UFRN)false
dc.title.pt_BR.fl_str_mv Influence of phosphate anions on the stability of immobilized enzymes. Effect of enzyme nature, immobilization protocol and inactivation conditions
title Influence of phosphate anions on the stability of immobilized enzymes. Effect of enzyme nature, immobilization protocol and inactivation conditions
spellingShingle Influence of phosphate anions on the stability of immobilized enzymes. Effect of enzyme nature, immobilization protocol and inactivation conditions
Kornecki, Jakub F.
Lipase interfacial activation
Enzyme destabilization
Immobilized enzyme stability
Buffers and enzyme stability
Tuning enzyme stability by immobilization
title_short Influence of phosphate anions on the stability of immobilized enzymes. Effect of enzyme nature, immobilization protocol and inactivation conditions
title_full Influence of phosphate anions on the stability of immobilized enzymes. Effect of enzyme nature, immobilization protocol and inactivation conditions
title_fullStr Influence of phosphate anions on the stability of immobilized enzymes. Effect of enzyme nature, immobilization protocol and inactivation conditions
title_full_unstemmed Influence of phosphate anions on the stability of immobilized enzymes. Effect of enzyme nature, immobilization protocol and inactivation conditions
title_sort Influence of phosphate anions on the stability of immobilized enzymes. Effect of enzyme nature, immobilization protocol and inactivation conditions
author Kornecki, Jakub F.
author_facet Kornecki, Jakub F.
Carballares, Diego
Sterlinga, Roberto Morellon
Siar, El Hocine
Kashefi, Saeid
Chafiaa, Mazri
Peña, Sara Arana
Rios, Nathalia Saraiva
Gonçalves, Luciana Rocha Barros
Lafuente, Roberto Fernandez
author_role author
author2 Carballares, Diego
Sterlinga, Roberto Morellon
Siar, El Hocine
Kashefi, Saeid
Chafiaa, Mazri
Peña, Sara Arana
Rios, Nathalia Saraiva
Gonçalves, Luciana Rocha Barros
Lafuente, Roberto Fernandez
author2_role author
author
author
author
author
author
author
author
author
dc.contributor.author.fl_str_mv Kornecki, Jakub F.
Carballares, Diego
Sterlinga, Roberto Morellon
Siar, El Hocine
Kashefi, Saeid
Chafiaa, Mazri
Peña, Sara Arana
Rios, Nathalia Saraiva
Gonçalves, Luciana Rocha Barros
Lafuente, Roberto Fernandez
dc.subject.por.fl_str_mv Lipase interfacial activation
Enzyme destabilization
Immobilized enzyme stability
Buffers and enzyme stability
Tuning enzyme stability by immobilization
topic Lipase interfacial activation
Enzyme destabilization
Immobilized enzyme stability
Buffers and enzyme stability
Tuning enzyme stability by immobilization
description 2030-12
publishDate 2020
dc.date.issued.fl_str_mv 2020-08
dc.date.accessioned.fl_str_mv 2021-11-29T21:30:36Z
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
format article
status_str publishedVersion
dc.identifier.citation.fl_str_mv KORNECKI, Jakub F.; CARBALLARES, Diego; MORELLON-STERLING, Roberto; SIAR, El Hocine; KASHEFI, Saeid; CHAFIAA, Mazri; ARANA-PEÑA, Sara; RIOS, Nathalia S.; GONÇALVES, Luciana R.B.; FERNANDEZ-LAFUENTE, Roberto. Influence of phosphate anions on the stability of immobilized enzymes. Effect of enzyme nature, immobilization protocol and inactivation conditions. Process Biochemistry, [S.L.], v. 95, p. 288-296, ago. 2020. Disponível em: https://www.sciencedirect.com/science/article/abs/pii/S1359511320301161?via%3Dihub#!. Acesso em: 29 nov. 2021.https://doi.org/10.1016/j.procbio.2020.02.025
dc.identifier.uri.fl_str_mv https://repositorio.ufrn.br/handle/123456789/45070
dc.identifier.issn.none.fl_str_mv 1359-5113
dc.identifier.doi.none.fl_str_mv 10.1016/j.procbio.2020.02.025
identifier_str_mv KORNECKI, Jakub F.; CARBALLARES, Diego; MORELLON-STERLING, Roberto; SIAR, El Hocine; KASHEFI, Saeid; CHAFIAA, Mazri; ARANA-PEÑA, Sara; RIOS, Nathalia S.; GONÇALVES, Luciana R.B.; FERNANDEZ-LAFUENTE, Roberto. Influence of phosphate anions on the stability of immobilized enzymes. Effect of enzyme nature, immobilization protocol and inactivation conditions. Process Biochemistry, [S.L.], v. 95, p. 288-296, ago. 2020. Disponível em: https://www.sciencedirect.com/science/article/abs/pii/S1359511320301161?via%3Dihub#!. Acesso em: 29 nov. 2021.https://doi.org/10.1016/j.procbio.2020.02.025
1359-5113
10.1016/j.procbio.2020.02.025
url https://repositorio.ufrn.br/handle/123456789/45070
dc.language.iso.fl_str_mv eng
language eng
dc.rights.driver.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:Repositório Institucional da UFRN
instname:Universidade Federal do Rio Grande do Norte (UFRN)
instacron:UFRN
instname_str Universidade Federal do Rio Grande do Norte (UFRN)
instacron_str UFRN
institution UFRN
reponame_str Repositório Institucional da UFRN
collection Repositório Institucional da UFRN
bitstream.url.fl_str_mv https://repositorio.ufrn.br/bitstream/123456789/45070/2/license_rdf
https://repositorio.ufrn.br/bitstream/123456789/45070/3/license.txt
bitstream.checksum.fl_str_mv 4d2950bda3d176f570a9f8b328dfbbef
6e6f57145bc87daf99079f06b081ff9f
bitstream.checksumAlgorithm.fl_str_mv MD5
MD5
repository.name.fl_str_mv Repositório Institucional da UFRN - Universidade Federal do Rio Grande do Norte (UFRN)
repository.mail.fl_str_mv
_version_ 1814832968548483072