Tuning Almond Lipase Features by Using Different Immobilization Supports

The lipase from Prunus dulcis almonds has been immobilized for the first time. For this purpose, two different supports, an octadecyl methacrylate particulate support, and aminated agarose (monoaminoethyl-N-aminoethyl) have been utilized. Both immobilized biocatalysts show improved enzyme stability,...

Descripción completa

Detalles Bibliográficos
Autores: Cherni, Oumaima, Carballares Navarro, Diego, Siar, El Hocine, Abellanas Pérez, Pedro, de Andrades, Diandra, Rocha Martín, Javier, Bahri, Sellema, Fernandez Lafuente, Roberto
Tipo de recurso: artículo
Fecha de publicación:2024
País:España
Institución:Universidad Complutense de Madrid (UCM)
Repositorio:Docta Complutense
Idioma:inglés
OAI Identifier:oai:docta.ucm.es:20.500.14352/119549
Acceso en línea:https://hdl.handle.net/20.500.14352/119549
Access Level:acceso abierto
Palabra clave:577.1
577.15
641.12
Lipase tuning by immobilization
Lipase tuning by buffers
Interfacially immobilized lipases
Ionically exchanged lipase
Bioquímica (Biología)
Alimentación
2403 Bioquímica
2302.09 Enzimología
2302.27 Proteínas
2302.90 Bioquímica de Alimentos
id ES_2fa665384e90aa8b4fc110ea380158f2
oai_identifier_str oai:docta.ucm.es:20.500.14352/119549
network_acronym_str ES
network_name_str España
repository_id_str
spelling Tuning Almond Lipase Features by Using Different Immobilization SupportsCherni, OumaimaCarballares Navarro, DiegoSiar, El HocineAbellanas Pérez, Pedrode Andrades, DiandraRocha Martín, JavierBahri, SellemaFernandez Lafuente, Roberto577.1577.15641.12Lipase tuning by immobilizationLipase tuning by buffersInterfacially immobilized lipasesIonically exchanged lipaseBioquímica (Biología)Alimentación2403 Bioquímica2302.09 Enzimología2302.27 Proteínas2302.90 Bioquímica de AlimentosThe lipase from Prunus dulcis almonds has been immobilized for the first time. For this purpose, two different supports, an octadecyl methacrylate particulate support, and aminated agarose (monoaminoethyl-N-aminoethyl) have been utilized. Both immobilized biocatalysts show improved enzyme stability, but great changes in enzyme specificity were detected. The enzyme immobilized via ion exchange maintained its activity intact versus p-nitrophenyl butyrate, while the enzyme immobilized on the hydrophobic support fully lost its activity versus this substrate, which was confirmed to be due to substrate adsorption on the support. However, this biocatalyst was much more active versus triacetin (more than 10-fold), R- or S- methyl mandelate at pH 7. At pH 9, a strong effect of using phosphate or bicarbonate as reaction buffers was detected. Using bicarbonate, the interfacially immobilized enzyme presented no activity versus R-isomer, but it was very active versus the S-isomer and triacetin. Using a phosphate buffer during the reaction, all compounds were recognized as substrates. The enzyme immobilized via ion exchange was significantly more active using phosphate; in fact, using bicarbonate, the enzyme was inactive versus both methyl mandelate isomers. This paper shows for the first time a great interaction between the effects of the immobilization protocol and buffer used during reaction on the enantiospecificity of lipases.MDPIUniversidad Complutense de Madrid20242024-01-3120242024-01-31journal articlehttp://purl.org/coar/resource_type/c_6501VoRhttp://purl.org/coar/version/c_970fb48d4fbd8a85info:eu-repo/semantics/articleapplication/pdfhttps://hdl.handle.net/20.500.14352/119549reponame:Docta Complutenseinstname:Universidad Complutense de Madrid (UCM)InglésengMIcinn Plan Estatal de Investigación Científica y Técnica y de Innovación 2021-2023 PID2022-136535OB-I00open accesshttp://purl.org/coar/access_right/c_abf2Attribution 4.0 Internationalhttp://creativecommons.org/licenses/by/4.0/info:eu-repo/semantics/openAccessoai:docta.ucm.es:20.500.14352/1195492026-06-02T12:44:21Z
dc.title.none.fl_str_mv Tuning Almond Lipase Features by Using Different Immobilization Supports
title Tuning Almond Lipase Features by Using Different Immobilization Supports
spellingShingle Tuning Almond Lipase Features by Using Different Immobilization Supports
Cherni, Oumaima
577.1
577.15
641.12
Lipase tuning by immobilization
Lipase tuning by buffers
Interfacially immobilized lipases
Ionically exchanged lipase
Bioquímica (Biología)
Alimentación
2403 Bioquímica
2302.09 Enzimología
2302.27 Proteínas
2302.90 Bioquímica de Alimentos
title_short Tuning Almond Lipase Features by Using Different Immobilization Supports
title_full Tuning Almond Lipase Features by Using Different Immobilization Supports
title_fullStr Tuning Almond Lipase Features by Using Different Immobilization Supports
title_full_unstemmed Tuning Almond Lipase Features by Using Different Immobilization Supports
title_sort Tuning Almond Lipase Features by Using Different Immobilization Supports
dc.creator.none.fl_str_mv Cherni, Oumaima
Carballares Navarro, Diego
Siar, El Hocine
Abellanas Pérez, Pedro
de Andrades, Diandra
Rocha Martín, Javier
Bahri, Sellema
Fernandez Lafuente, Roberto
author Cherni, Oumaima
author_facet Cherni, Oumaima
Carballares Navarro, Diego
Siar, El Hocine
Abellanas Pérez, Pedro
de Andrades, Diandra
Rocha Martín, Javier
Bahri, Sellema
Fernandez Lafuente, Roberto
author_role author
author2 Carballares Navarro, Diego
Siar, El Hocine
Abellanas Pérez, Pedro
de Andrades, Diandra
Rocha Martín, Javier
Bahri, Sellema
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 577.1
577.15
641.12
Lipase tuning by immobilization
Lipase tuning by buffers
Interfacially immobilized lipases
Ionically exchanged lipase
Bioquímica (Biología)
Alimentación
2403 Bioquímica
2302.09 Enzimología
2302.27 Proteínas
2302.90 Bioquímica de Alimentos
topic 577.1
577.15
641.12
Lipase tuning by immobilization
Lipase tuning by buffers
Interfacially immobilized lipases
Ionically exchanged lipase
Bioquímica (Biología)
Alimentación
2403 Bioquímica
2302.09 Enzimología
2302.27 Proteínas
2302.90 Bioquímica de Alimentos
description The lipase from Prunus dulcis almonds has been immobilized for the first time. For this purpose, two different supports, an octadecyl methacrylate particulate support, and aminated agarose (monoaminoethyl-N-aminoethyl) have been utilized. Both immobilized biocatalysts show improved enzyme stability, but great changes in enzyme specificity were detected. The enzyme immobilized via ion exchange maintained its activity intact versus p-nitrophenyl butyrate, while the enzyme immobilized on the hydrophobic support fully lost its activity versus this substrate, which was confirmed to be due to substrate adsorption on the support. However, this biocatalyst was much more active versus triacetin (more than 10-fold), R- or S- methyl mandelate at pH 7. At pH 9, a strong effect of using phosphate or bicarbonate as reaction buffers was detected. Using bicarbonate, the interfacially immobilized enzyme presented no activity versus R-isomer, but it was very active versus the S-isomer and triacetin. Using a phosphate buffer during the reaction, all compounds were recognized as substrates. The enzyme immobilized via ion exchange was significantly more active using phosphate; in fact, using bicarbonate, the enzyme was inactive versus both methyl mandelate isomers. This paper shows for the first time a great interaction between the effects of the immobilization protocol and buffer used during reaction on the enantiospecificity of lipases.
publishDate 2024
dc.date.none.fl_str_mv 2024
2024-01-31
2024
2024-01-31
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/20.500.14352/119549
url https://hdl.handle.net/20.500.14352/119549
dc.language.none.fl_str_mv Inglés
eng
language_invalid_str_mv Inglés
language eng
dc.relation.none.fl_str_mv MIcinn Plan Estatal de Investigación Científica y Técnica y de Innovación 2021-2023 PID2022-136535OB-I00
dc.rights.none.fl_str_mv open access
http://purl.org/coar/access_right/c_abf2
Attribution 4.0 International
http://creativecommons.org/licenses/by/4.0/
dc.rights.openaire.fl_str_mv info:eu-repo/semantics/openAccess
rights_invalid_str_mv open access
http://purl.org/coar/access_right/c_abf2
Attribution 4.0 International
http://creativecommons.org/licenses/by/4.0/
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv MDPI
publisher.none.fl_str_mv MDPI
dc.source.none.fl_str_mv reponame:Docta Complutense
instname:Universidad Complutense de Madrid (UCM)
instname_str Universidad Complutense de Madrid (UCM)
reponame_str Docta Complutense
collection Docta Complutense
repository.name.fl_str_mv
repository.mail.fl_str_mv
_version_ 1869405491908575232
score 15.81155

Similares en LA Referencia