Influence of phosphate anions on the stability of immobilized enzymes. Effect of enzyme nature, immobilization protocol and inactivation conditions
Autor(a) principal: | |
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Data de Publicação: | 2020 |
Outros Autores: | , , , , , , , , |
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 |
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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 |
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Elsevier |
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Elsevier |
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