A review on the immobilization of pepsin: A Lys-poor enzyme that is unstable at alkaline pH values
Pepsin is a protease used in many different applications, and in many instances, it is utilized in an immobilized form to prevent contamination of the reaction product. This enzyme has two peculiarities that make its immobilization complex. The first one is related to the poor presence of primary am...
| Autores: | , , , , , , , |
|---|---|
| Tipo de recurso: | artículo |
| Fecha de publicación: | 2022 |
| País: | España |
| Institución: | Universidad Complutense de Madrid (UCM) |
| Repositorio: | Docta Complutense |
| Idioma: | inglés |
| OAI Identifier: | oai:docta.ucm.es:20.500.14352/101578 |
| Acceso en línea: | https://hdl.handle.net/20.500.14352/101578 |
| Access Level: | acceso abierto |
| Palabra clave: | 66.0 620 Multi-point covalent immobilization Ion exchange Glutaraldehyde versatility Ingeniería química Química industrial Bioquímica (Química) 2302 Bioquímica 3302 Tecnología Bioquímica 3303 Ingeniería y Tecnología Químicas |
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A review on the immobilization of pepsin: A Lys-poor enzyme that is unstable at alkaline pH valuesMorellon-Sterling, RobertoTavano, OlgaBolívar Bolívar, Juan ManuelBerenguer-Murcia, ÁngelVela-Gutiérrez, GilberSabir, JamalTacias-Pascacio, VeymarFernandez-Lafuente, Roberto66.0620Multi-point covalent immobilizationIon exchangeGlutaraldehyde versatilityIngeniería químicaQuímica industrialBioquímica (Química)2302 Bioquímica3302 Tecnología Bioquímica3303 Ingeniería y Tecnología QuímicasPepsin is a protease used in many different applications, and in many instances, it is utilized in an immobilized form to prevent contamination of the reaction product. This enzyme has two peculiarities that make its immobilization complex. The first one is related to the poor presence of primary amino groups on its surface (just one Lys and the terminal amino group). The second one is its poor stability at alkaline pH values. Both features make the immobilization of this enzyme to be considered a complicated goal, as most of the immobilization protocols utilize primary amino groups for immobilization. This review presents some of the attempts to get immobilized pepsin biocatalyst and their applications. The high density of anionic groups (Asp and Glu) make the anion exchange of the enzyme simpler, but this makes many of the strategies utilized to immobilize the enzyme (e.g., amino-glutaraldehyde supports) more related to a mixed ion exchange/hydrophobic adsorption than to real covalent immobilization. Finally, we propose some possibilities that can permit not only the covalent immobilization of this enzyme, but also their stabilization via multipoint covalent attachment.ElsevierUniversidad Complutense de Madrid20222022-01-0120222022-01-01journal articlehttp://purl.org/coar/resource_type/c_6501VoRhttp://purl.org/coar/version/c_970fb48d4fbd8a85info:eu-repo/semantics/articleapplication/pdfhttps://hdl.handle.net/20.500.14352/101578reponame:Docta Complutenseinstname:Universidad Complutense de Madrid (UCM)InglésengAgencia Estatal de Investigación http://dx.doi.org/10.13039/501100011033 Plan Estatal de Investigación Científica y Técnica y de Innovación 2013-2016 CTQ2017-86170-R DISEÑO DE ESTRATEGIAS PARA LA PRODUCCION DE CATALIZADORES CON ENZIMAS COINMOVILIZADAS Y SU EMPLEO EN REACCIONES EN CASCADAAgencia Estatal de Investigación http://dx.doi.org/10.13039/501100011033 Plan Estatal de Investigación Científica y Técnica y de Innovación 2017-2020 RTI2018-095291-B-I00 APROVECHAMIENTO MAS EFICIENTE DE BIOMASA LIGNOCELULOSICA PARA LA OBTENCION DE MATERIALES CARBONOSOS DE ALTAS PRESTACIONES Y PRODUCTOS QUIMICOSopen accesshttp://purl.org/coar/access_right/c_abf2Attribution-NonCommercial-NoDerivatives 4.0 Internationalhttp://creativecommons.org/licenses/by-nc-nd/4.0/info:eu-repo/semantics/openAccessoai:docta.ucm.es:20.500.14352/1015782026-06-02T12:44:21Z |
| dc.title.none.fl_str_mv |
A review on the immobilization of pepsin: A Lys-poor enzyme that is unstable at alkaline pH values |
| title |
A review on the immobilization of pepsin: A Lys-poor enzyme that is unstable at alkaline pH values |
| spellingShingle |
A review on the immobilization of pepsin: A Lys-poor enzyme that is unstable at alkaline pH values Morellon-Sterling, Roberto 66.0 620 Multi-point covalent immobilization Ion exchange Glutaraldehyde versatility Ingeniería química Química industrial Bioquímica (Química) 2302 Bioquímica 3302 Tecnología Bioquímica 3303 Ingeniería y Tecnología Químicas |
| title_short |
A review on the immobilization of pepsin: A Lys-poor enzyme that is unstable at alkaline pH values |
| title_full |
A review on the immobilization of pepsin: A Lys-poor enzyme that is unstable at alkaline pH values |
| title_fullStr |
A review on the immobilization of pepsin: A Lys-poor enzyme that is unstable at alkaline pH values |
| title_full_unstemmed |
A review on the immobilization of pepsin: A Lys-poor enzyme that is unstable at alkaline pH values |
| title_sort |
A review on the immobilization of pepsin: A Lys-poor enzyme that is unstable at alkaline pH values |
| dc.creator.none.fl_str_mv |
Morellon-Sterling, Roberto Tavano, Olga Bolívar Bolívar, Juan Manuel Berenguer-Murcia, Ángel Vela-Gutiérrez, Gilber Sabir, Jamal Tacias-Pascacio, Veymar Fernandez-Lafuente, Roberto |
| author |
Morellon-Sterling, Roberto |
| author_facet |
Morellon-Sterling, Roberto Tavano, Olga Bolívar Bolívar, Juan Manuel Berenguer-Murcia, Ángel Vela-Gutiérrez, Gilber Sabir, Jamal Tacias-Pascacio, Veymar Fernandez-Lafuente, Roberto |
| author_role |
author |
| author2 |
Tavano, Olga Bolívar Bolívar, Juan Manuel Berenguer-Murcia, Ángel Vela-Gutiérrez, Gilber Sabir, Jamal Tacias-Pascacio, Veymar Fernandez-Lafuente, Roberto |
| author2_role |
author author author author author author author |
| dc.contributor.none.fl_str_mv |
Universidad Complutense de Madrid |
| dc.subject.none.fl_str_mv |
66.0 620 Multi-point covalent immobilization Ion exchange Glutaraldehyde versatility Ingeniería química Química industrial Bioquímica (Química) 2302 Bioquímica 3302 Tecnología Bioquímica 3303 Ingeniería y Tecnología Químicas |
| topic |
66.0 620 Multi-point covalent immobilization Ion exchange Glutaraldehyde versatility Ingeniería química Química industrial Bioquímica (Química) 2302 Bioquímica 3302 Tecnología Bioquímica 3303 Ingeniería y Tecnología Químicas |
| description |
Pepsin is a protease used in many different applications, and in many instances, it is utilized in an immobilized form to prevent contamination of the reaction product. This enzyme has two peculiarities that make its immobilization complex. The first one is related to the poor presence of primary amino groups on its surface (just one Lys and the terminal amino group). The second one is its poor stability at alkaline pH values. Both features make the immobilization of this enzyme to be considered a complicated goal, as most of the immobilization protocols utilize primary amino groups for immobilization. This review presents some of the attempts to get immobilized pepsin biocatalyst and their applications. The high density of anionic groups (Asp and Glu) make the anion exchange of the enzyme simpler, but this makes many of the strategies utilized to immobilize the enzyme (e.g., amino-glutaraldehyde supports) more related to a mixed ion exchange/hydrophobic adsorption than to real covalent immobilization. Finally, we propose some possibilities that can permit not only the covalent immobilization of this enzyme, but also their stabilization via multipoint covalent attachment. |
| publishDate |
2022 |
| dc.date.none.fl_str_mv |
2022 2022-01-01 2022 2022-01-01 |
| dc.type.none.fl_str_mv |
journal article http://purl.org/coar/resource_type/c_6501 VoR http://purl.org/coar/version/c_970fb48d4fbd8a85 |
| dc.type.openaire.fl_str_mv |
info:eu-repo/semantics/article |
| format |
article |
| dc.identifier.none.fl_str_mv |
https://hdl.handle.net/20.500.14352/101578 |
| url |
https://hdl.handle.net/20.500.14352/101578 |
| dc.language.none.fl_str_mv |
Inglés eng |
| language_invalid_str_mv |
Inglés |
| language |
eng |
| dc.relation.none.fl_str_mv |
Agencia Estatal de Investigación http://dx.doi.org/10.13039/501100011033 Plan Estatal de Investigación Científica y Técnica y de Innovación 2013-2016 CTQ2017-86170-R DISEÑO DE ESTRATEGIAS PARA LA PRODUCCION DE CATALIZADORES CON ENZIMAS COINMOVILIZADAS Y SU EMPLEO EN REACCIONES EN CASCADA Agencia Estatal de Investigación http://dx.doi.org/10.13039/501100011033 Plan Estatal de Investigación Científica y Técnica y de Innovación 2017-2020 RTI2018-095291-B-I00 APROVECHAMIENTO MAS EFICIENTE DE BIOMASA LIGNOCELULOSICA PARA LA OBTENCION DE MATERIALES CARBONOSOS DE ALTAS PRESTACIONES Y PRODUCTOS QUIMICOS |
| dc.rights.none.fl_str_mv |
open access http://purl.org/coar/access_right/c_abf2 Attribution-NonCommercial-NoDerivatives 4.0 International http://creativecommons.org/licenses/by-nc-nd/4.0/ |
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info:eu-repo/semantics/openAccess |
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open access http://purl.org/coar/access_right/c_abf2 Attribution-NonCommercial-NoDerivatives 4.0 International http://creativecommons.org/licenses/by-nc-nd/4.0/ |
| eu_rights_str_mv |
openAccess |
| dc.format.none.fl_str_mv |
application/pdf |
| dc.publisher.none.fl_str_mv |
Elsevier |
| publisher.none.fl_str_mv |
Elsevier |
| dc.source.none.fl_str_mv |
reponame:Docta Complutense instname:Universidad Complutense de Madrid (UCM) |
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Universidad Complutense de Madrid (UCM) |
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Docta Complutense |
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Docta Complutense |
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