Novozym 435: The "perfect" lipase immobilized biocatalyst?

Autores
Ortiz, Claudia Susana; Ferreira, María Luján; Barbosa, Oveimar; dos Santos, Jose C. S.; Rodrigues, Rafael C.; Berenguer Murcia, Ángel; Briand, Laura Estefania; Fernandez Lafuente, Roberto
Año de publicación
2019
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Novozym 435 (N435) is a commercially available immobilized lipase produced by Novozymes. It is based on immobilization via interfacial activation of lipase B from Candida antarctica on a resin, Lewatit VP OC 1600. This resin is a macroporous support formed by poly(methyl methacrylate) crosslinked with divinylbenzene. N435 is perhaps the most widely used commercial biocatalyst in both academy and industry. Here, we review some of the success stories of N435 (in chemistry, energy and lipid manipulation), but we focus on some of the problems that the use of this biocatalyst may generate. Some of these problems are just based on the mechanism of immobilization (interfacial activation) that may facilitate enzyme desorption under certain conditions. Other problems are specific to the support: Mechanical fragility, moderate hydrophilicity that permits the accumulation of hydrophilic compounds (e.g., water or glycerin) and the most critical one, support dissolution in some organic media. Finally, some solutions (N435 coating with silicone, enzyme physical or chemical crosslinking, and use of alternative supports) are proposed. However, the N435 history, even with these problems, may continue in the coming future due to its very good properties if some simpler alternative biocatalysts are not developed.
Fil: Ortiz, Claudia Susana. Universidad Industrial Santander; Colombia
Fil: Ferreira, María Luján. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Planta Piloto de Ingeniería Química. Universidad Nacional del Sur. Planta Piloto de Ingeniería Química; Argentina
Fil: Barbosa, Oveimar. Universidad del Tolima. Facultad de Ciencias Exactas; Colombia
Fil: dos Santos, Jose C. S.. Universidade Da Integracao Internacional Da Lusofonia Afrobrasileira.; Brasil
Fil: Rodrigues, Rafael C.. Universidade Federal do Rio Grande do Sul; Brasil
Fil: Berenguer Murcia, Ángel. Universidad de Alicante. Facultad de Ciencias. Departamento de Quimica Inorganica.; España
Fil: Briand, Laura Estefania. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Ciencias Aplicadas "Dr. Jorge J. Ronco". Universidad Nacional de la Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Ciencias Aplicadas; Argentina
Fil: Fernandez Lafuente, Roberto. Consejo Superior de Investigaciones Científicas. Instituto de Catálisis y Petroleoquímica; España
Materia
LIPASE
NOVOZYM 435
SUPPORT BREAKAGE
ENZYME LEACHING
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/141746
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/141746
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Novozym 435: The "perfect" lipase immobilized biocatalyst?Ortiz, Claudia SusanaFerreira, María LujánBarbosa, Oveimardos Santos, Jose C. S.Rodrigues, Rafael C.Berenguer Murcia, ÁngelBriand, Laura EstefaniaFernandez Lafuente, RobertoLIPASENOVOZYM 435SUPPORT BREAKAGEENZYME LEACHINGhttps://purl.org/becyt/ford/2.9https://purl.org/becyt/ford/2Novozym 435 (N435) is a commercially available immobilized lipase produced by Novozymes. It is based on immobilization via interfacial activation of lipase B from Candida antarctica on a resin, Lewatit VP OC 1600. This resin is a macroporous support formed by poly(methyl methacrylate) crosslinked with divinylbenzene. N435 is perhaps the most widely used commercial biocatalyst in both academy and industry. Here, we review some of the success stories of N435 (in chemistry, energy and lipid manipulation), but we focus on some of the problems that the use of this biocatalyst may generate. Some of these problems are just based on the mechanism of immobilization (interfacial activation) that may facilitate enzyme desorption under certain conditions. Other problems are specific to the support: Mechanical fragility, moderate hydrophilicity that permits the accumulation of hydrophilic compounds (e.g., water or glycerin) and the most critical one, support dissolution in some organic media. Finally, some solutions (N435 coating with silicone, enzyme physical or chemical crosslinking, and use of alternative supports) are proposed. However, the N435 history, even with these problems, may continue in the coming future due to its very good properties if some simpler alternative biocatalysts are not developed.Fil: Ortiz, Claudia Susana. Universidad Industrial Santander; ColombiaFil: Ferreira, María Luján. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Planta Piloto de Ingeniería Química. Universidad Nacional del Sur. Planta Piloto de Ingeniería Química; ArgentinaFil: Barbosa, Oveimar. Universidad del Tolima. Facultad de Ciencias Exactas; ColombiaFil: dos Santos, Jose C. S.. Universidade Da Integracao Internacional Da Lusofonia Afrobrasileira.; BrasilFil: Rodrigues, Rafael C.. Universidade Federal do Rio Grande do Sul; BrasilFil: Berenguer Murcia, Ángel. Universidad de Alicante. Facultad de Ciencias. Departamento de Quimica Inorganica.; EspañaFil: Briand, Laura Estefania. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Ciencias Aplicadas "Dr. Jorge J. Ronco". Universidad Nacional de la Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Ciencias Aplicadas; ArgentinaFil: Fernandez Lafuente, Roberto. Consejo Superior de Investigaciones Científicas. Instituto de Catálisis y Petroleoquímica; EspañaRoyal Society of Chemistry2019-04-12info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/141746Ortiz, Claudia Susana; Ferreira, María Luján; Barbosa, Oveimar; dos Santos, Jose C. S.; Rodrigues, Rafael C.; et al.; Novozym 435: The "perfect" lipase immobilized biocatalyst?; Royal Society of Chemistry; Catalysis Science and Technology; 9; 10; 12-4-2019; 2380-24202044-47532044-4761CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/http://pubs.rsc.org/en/Content/ArticleLanding/2019/CY/C9CY00415Ginfo:eu-repo/semantics/altIdentifier/doi/10.1039/C9CY00415Ginfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:24:38Zoai:ri.conicet.gov.ar:11336/141746instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-29 10:24:39.247CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Novozym 435: The "perfect" lipase immobilized biocatalyst?
title Novozym 435: The "perfect" lipase immobilized biocatalyst?
spellingShingle Novozym 435: The "perfect" lipase immobilized biocatalyst?
Ortiz, Claudia Susana
LIPASE
NOVOZYM 435
SUPPORT BREAKAGE
ENZYME LEACHING
title_short Novozym 435: The "perfect" lipase immobilized biocatalyst?
title_full Novozym 435: The "perfect" lipase immobilized biocatalyst?
title_fullStr Novozym 435: The "perfect" lipase immobilized biocatalyst?
title_full_unstemmed Novozym 435: The "perfect" lipase immobilized biocatalyst?
title_sort Novozym 435: The "perfect" lipase immobilized biocatalyst?
dc.creator.none.fl_str_mv Ortiz, Claudia Susana
Ferreira, María Luján
Barbosa, Oveimar
dos Santos, Jose C. S.
Rodrigues, Rafael C.
Berenguer Murcia, Ángel
Briand, Laura Estefania
Fernandez Lafuente, Roberto
author Ortiz, Claudia Susana
author_facet Ortiz, Claudia Susana
Ferreira, María Luján
Barbosa, Oveimar
dos Santos, Jose C. S.
Rodrigues, Rafael C.
Berenguer Murcia, Ángel
Briand, Laura Estefania
Fernandez Lafuente, Roberto
author_role author
author2 Ferreira, María Luján
Barbosa, Oveimar
dos Santos, Jose C. S.
Rodrigues, Rafael C.
Berenguer Murcia, Ángel
Briand, Laura Estefania
Fernandez Lafuente, Roberto
author2_role author
author
author
author
author
author
author
dc.subject.none.fl_str_mv LIPASE
NOVOZYM 435
SUPPORT BREAKAGE
ENZYME LEACHING
topic LIPASE
NOVOZYM 435
SUPPORT BREAKAGE
ENZYME LEACHING
purl_subject.fl_str_mv https://purl.org/becyt/ford/2.9
https://purl.org/becyt/ford/2
dc.description.none.fl_txt_mv Novozym 435 (N435) is a commercially available immobilized lipase produced by Novozymes. It is based on immobilization via interfacial activation of lipase B from Candida antarctica on a resin, Lewatit VP OC 1600. This resin is a macroporous support formed by poly(methyl methacrylate) crosslinked with divinylbenzene. N435 is perhaps the most widely used commercial biocatalyst in both academy and industry. Here, we review some of the success stories of N435 (in chemistry, energy and lipid manipulation), but we focus on some of the problems that the use of this biocatalyst may generate. Some of these problems are just based on the mechanism of immobilization (interfacial activation) that may facilitate enzyme desorption under certain conditions. Other problems are specific to the support: Mechanical fragility, moderate hydrophilicity that permits the accumulation of hydrophilic compounds (e.g., water or glycerin) and the most critical one, support dissolution in some organic media. Finally, some solutions (N435 coating with silicone, enzyme physical or chemical crosslinking, and use of alternative supports) are proposed. However, the N435 history, even with these problems, may continue in the coming future due to its very good properties if some simpler alternative biocatalysts are not developed.
Fil: Ortiz, Claudia Susana. Universidad Industrial Santander; Colombia
Fil: Ferreira, María Luján. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Planta Piloto de Ingeniería Química. Universidad Nacional del Sur. Planta Piloto de Ingeniería Química; Argentina
Fil: Barbosa, Oveimar. Universidad del Tolima. Facultad de Ciencias Exactas; Colombia
Fil: dos Santos, Jose C. S.. Universidade Da Integracao Internacional Da Lusofonia Afrobrasileira.; Brasil
Fil: Rodrigues, Rafael C.. Universidade Federal do Rio Grande do Sul; Brasil
Fil: Berenguer Murcia, Ángel. Universidad de Alicante. Facultad de Ciencias. Departamento de Quimica Inorganica.; España
Fil: Briand, Laura Estefania. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Ciencias Aplicadas "Dr. Jorge J. Ronco". Universidad Nacional de la Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Ciencias Aplicadas; Argentina
Fil: Fernandez Lafuente, Roberto. Consejo Superior de Investigaciones Científicas. Instituto de Catálisis y Petroleoquímica; España
description Novozym 435 (N435) is a commercially available immobilized lipase produced by Novozymes. It is based on immobilization via interfacial activation of lipase B from Candida antarctica on a resin, Lewatit VP OC 1600. This resin is a macroporous support formed by poly(methyl methacrylate) crosslinked with divinylbenzene. N435 is perhaps the most widely used commercial biocatalyst in both academy and industry. Here, we review some of the success stories of N435 (in chemistry, energy and lipid manipulation), but we focus on some of the problems that the use of this biocatalyst may generate. Some of these problems are just based on the mechanism of immobilization (interfacial activation) that may facilitate enzyme desorption under certain conditions. Other problems are specific to the support: Mechanical fragility, moderate hydrophilicity that permits the accumulation of hydrophilic compounds (e.g., water or glycerin) and the most critical one, support dissolution in some organic media. Finally, some solutions (N435 coating with silicone, enzyme physical or chemical crosslinking, and use of alternative supports) are proposed. However, the N435 history, even with these problems, may continue in the coming future due to its very good properties if some simpler alternative biocatalysts are not developed.
publishDate 2019
dc.date.none.fl_str_mv 2019-04-12
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/141746
Ortiz, Claudia Susana; Ferreira, María Luján; Barbosa, Oveimar; dos Santos, Jose C. S.; Rodrigues, Rafael C.; et al.; Novozym 435: The "perfect" lipase immobilized biocatalyst?; Royal Society of Chemistry; Catalysis Science and Technology; 9; 10; 12-4-2019; 2380-2420
2044-4753
2044-4761
CONICET Digital
CONICET
url http://hdl.handle.net/11336/141746
identifier_str_mv Ortiz, Claudia Susana; Ferreira, María Luján; Barbosa, Oveimar; dos Santos, Jose C. S.; Rodrigues, Rafael C.; et al.; Novozym 435: The "perfect" lipase immobilized biocatalyst?; Royal Society of Chemistry; Catalysis Science and Technology; 9; 10; 12-4-2019; 2380-2420
2044-4753
2044-4761
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://pubs.rsc.org/en/Content/ArticleLanding/2019/CY/C9CY00415G
info:eu-repo/semantics/altIdentifier/doi/10.1039/C9CY00415G
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Royal Society of Chemistry
publisher.none.fl_str_mv Royal Society of Chemistry
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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score 13.069144

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