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
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/141746
Ver los metadatos del registro completo
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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 Técnicas2025-09-03T10:04:47Zoai: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:34982025-09-03 10:04:48.158CONICET 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 |
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CONICET Digital (CONICET) |
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Consejo Nacional de Investigaciones Científicas y Técnicas |
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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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1842269876390985728 |
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13.13397 |